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July 30, 2005

Virtual Screening, Docking & Scoring Program

Specific binding interactions are central to many biological processes and pathways. Similarly, most drugs act by binding specifically to a site on a target protein, thereby modulating protein activity. The quest for new drugs relies on many approaches, including computer-based docking. This computational approach has the potential to have a profound positive impact on drug discovery, justifying the keen interest in this field by pharmaceutical researchers. Over the past fifteen years, subsequent to the initial description of the DOCK program and in parallel with the exponential increase in the number of available high-resolution protein structures, many docking programs of use as virtual screening tools in the drug discovery process have emerged. Understanding the similarities and differences of different methods as well as their capabilities and limitations is both important and increasingly challenging.

The main objective of our "Virtual Screening, Docking and Scoring" program is to foster discussion amongst researchers working on both development of screening and docking methods and the application of such methods to drug discovery. This interaction will lead to a better understanding of the current state-of-the-art, improved screening and docking tools in the future, and enhanced awareness of how to apply the current set of tools.

We are holding InterAction Meeting sessions at Bryn Mawr College, Philadelphia on 11 October ’05 and in Basel, Switzerland on 9 November ’05 on Virtual Screening, Docking and Scoring.  The purpose of the meetings is to bring together world-class researchers working in the computational screening and docking area, and have them present and discuss recent and new results in cutting-edge research areas relevant to drug discovery. The emphasis of the meeting activity is on communication and open discussion, which we hope will lead to new ideas and collaborations towards progress and innovation in the disease areas discussed.  A significant amount of time at the meeting will be devoted to question time and panel and group discussions towards this goal.

A description of the session and invited speaker presentations with abstracts follows:

eCheminfo InterAction Meeting Session, Philadelphia, 11 October 2005

Virtual Screening, Docking & Scoring
chaired by Max Cummings (Johnson & Johnson)
eCheminfo 2005 US InterAction Meeting, 11-12 October 2005, Philadelphia, USA
Program Updates loaded in the Program Areas on http://echeminfo.com/

Invited Speakers & Discussion Leaders:
Reducing false positives in virtual screens on kinase targets, Emanuele Perola (Vertex)
New Docking Methods for Pose Prediction and Enrichment, Mark McGann (Openeye)
Molecular Docking as a Virtual Screening Tool, Renee DesJarlais (Johnson & Johnson)
Exploiting protein-specific information in docking, Willem Nissink (Cambridge Crystallographic Data Centre)
You can't find what's not there: the importance and the pitfalls of multiple representations of molecules in dockable databases, John Irwin (UCSF)

eCheminfo InterAction Meeting Session, Basel, 9 November 2005
Virtual Screening, Docking & Scoring
chaired by Miklos Vargyas (ChemAxon)
eCheminfo 2005 European InterAction Meeting, 9-10 November 2005, Basel, Switzerland
Program Updates loaded in the Program Areas on http://echeminfo.com/

Invited Speakers & Discussion Leaders:
Pattern Recognition and Grid Computing in Drug Discovery, Graham Richards (University of Oxford)
The Issue of Protein Flexibility in Docking-Based Virtual Screening, Xavier Barril (Vernalis)
Discovery of cell-permeable nonpeptide inhibitors of beta-secretase by high-throughput docking and continuum electrostatic calculations, Amedeo Caflisch (University of Zurich)
Beyond ligand flexibility: improvement and validation of rDock for Structure-Based Drug Design, David Morley (Enspiral Discovery Ltd)
Structure-based identification of GPCR ligands by high-throughput docking, Didier Rognan (University of Strasbourg)

[COMPLETE ABSTRACTS FOLLOW IN REMAINDER OF POST]

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CFP: Posters, Contributed talks, Bursaries for eCheminfo Autumn meetings on Drug Discovery

Poster Abstracts for eCheminfo Autumn InterAction Meetings should be submitted as soon as possible and at the latest by: 15 August ’05 for US meeting posters; 31 August ’05 for European meeting posters.

Posters can be on any informatics or modeling topic (and can also be combined with experimental approaches) of relevance to Drug Discovery.

Poster Abstracts (ca. 300 words) should be sent to eCheminfo at douglasconnect.com

We will select a number of contributed talks to be presented at the meetings based on abstracts submitted.  We also have sponsorship requests under review to support travel bursaries for a selection of young academic investigators to attend the meeting based on submitted abstract.

Papers submitted related to poster presentations or talks will be refereed for consideration for publication in a special Drug Discovery issue of the Molecular Simulation journal.  Deadline for paper submission: 31 October ’05 for US meeting; 30 November ’05 for European meeting posters.

Subscribed members who cannot attend the meetings in Philadelphia or Basel in person will be able to access all meeting presentations with audio and to submit posters through the eCheminfo website. 

You must also have completed your annual membership subscription or meeting registration in time through the Online Ticket Office available after login to http://echeminfo.com/ so that access rights or a meeting place reservation are provided for you.   Alternatively contact Nicki Douglas (nicki.douglas at douglasconnect.com, +41 61 851 0461) for support.  Academic and group rates are available.

Barry Hardy
eCheminfo Community of Practice Manager
Douglas Connect, Switzerland
+41 61 851 0170 (office)

eCheminfo US Autumn 2005 InterAction Meeting:  Applications of Cheminformatics & Chemical Modelling to Drug Discovery
October 11-12, Bryn Mawr College, Philadelphia, USA
and
eCheminfo European Autumn 2005 InterAction Meeting:  Applications of Cheminformatics & Chemical Modelling to Drug Discovery
November 9-10, Swissotel L’entrée Conference Center, Basel, Switzerland

You can view meeting abstracts in the Program area of http://echeminfo.com/

July 23, 2005

Web-based Services in Drug Discovery

Pharmaceutical research is under challenge to improve the choice, quality and safety of lead candidates. There is a clear need for an open discussion and an awareness of the requirements for a much more complex knowledge management and knowledge transfer between academic, government and commercial interests. The semantic web has the potential to make significant contributions to the drug discovery of the future but is at this time at an early development stage and there are only a few public tools for the data mining and sharing of chemical information.

Just a few years ago, the only imaginable way of doing in silico drug design - or, indeed, any cheminformatics research - was to use in-house and commercial software and databases. New developments in Web services however are offering today’s researchers additional resources. Although cheminformatics admittedly lags far behind bioinformatics (where an enormous wealth of data and software is literally a click away), we are beginning to see some chemical resources in open access.

A goal for this eCheminfo program on "Web-based Services in Drug Design" is to present some of the possibilities of web-based tools and data and to lead into discussions on how can web services work for both the academic world and industry, while maintaining commercial, ip and security concerns? What potential impact could they have on discovery productivity? What are the best sustainable business models that can be applied to such services? How significant are the benefits of increased upstream and downstream knowledge flow due to services based on ontology frameworks? What are the key current hindrances to be overcome for the integration of web services into drug discovery in the chemical information area?

We are convening the following community of practice meeting sessions  to both present the latest research advances in this area and to discuss the above issues.  (As with all our meetings, if you cannot make the meetings you can access the seminars and discussions through the eCheminfo website by signing up for community membership.)

Applications of Web-based Services in Drug Discovery
eCheminfo InterAction Meeting Session, Philadelphia, 11 October 2005
chaired by Marc Nicklaus, (National Institutes of Health)
eCheminfo 2005 InterAction Meeting, 11-12 October 2005, Philadelphia, USA

Presenters & Discussion Leaders:
A Web-based Chemoinformatics System for Drug Discovery, Brett Tounge (Johnson & Johnson)
Web enabling technology for the design, enumeration, optimization and tracking of compound libraries, Brad Feuston (Merck)
ZINC web services - providing 3D structures of purchasable compounds for virtual screening to humans and machines, John Irwin (UCSF)
Pubchem, Steve Bryant (NCBI)
Search-and-query Information System for the Study and Discovery of Novel Agents in the Treatment of Cancer, David Covell (NCI)
Title TBA, Dmitrii Rassokhin (Johnson & Johnson)

Applications of Web-based Services in Drug Discovery

eCheminfo InterAction Meeting Session, Basel, 10 November 2005
chaired by Kim Henrick (European Bioinformatics Institute)
eCheminfo 2005 InterAction Meeting, 9-10 November 2005, Basel, Switzerland

Presenters & Discussion Leaders:

Investigating chemical trends in the context of ligand-protein complexes by using on-line data analysis directly on the web, Dimitris Dimitropoulos (European Bioinformatics Institute)
The Representation of Chemical Structures and its Application to Property Prediction, Johann Gasteiger (Universitaet Erlangen-Nuernberg)
Open Archives as a Route for the Capture, Dissemination and Access to Chemical Information, Simon Coles (University of Southampton)
Identification of biological units in protein crystals, Eugene Krissinel (European Bioinformatics Institute)
SWISS-MODEL Server and Repository: Web based resources for comparative protein structure modeling and their application in drug discovery, Torsten Schwede (University of Basel)

ABSTRACTS

PHILADELPHIA SESSION

A Web-based Chemoinformatics System for Drug Discovery

Brett A. Tounge, Johnson & Johnson Pharmaceutical Research and Development, L.L.C., Welsh and McKean Roads, PO Box 776, Spring House, PA 19477, USA

One of the key questions that must be addressed when implementing a chemoinformatics system is whether the tools will be designed for use by the expert user or by the “bench scientist”.  This decision can impact not only the style of tools that are rolled out, but is also a factor in terms of how these tools are delivered to the end users.  The system that we outline here was designed for use by the non-expert user.  As such, the tools that we discuss are in many cases simplified versions of some common algorithms used in chemoinformatics.  In addition, the focus is on how to distribute these tools using a web services interface, which greatly simplifies delivering new protocols to the end user.

Web enabling technology for the design, enumeration, optimization and tracking of compound libraries

Bradley P. Feuston(1)*,Subhas J. Chakravorty(1), John F. Conway(3),J. Christopher Culberson(1), Joseph Forbes(1), Bryan Kraker(2), Patricia A. Lennon(3), Craig Lindsley(5), Georgia B. McGaughey(1), Ralph Mosley(2), Robert P. Sheridan(2), Mario Valenciano(4) and Simon K. Kearsley(2)

(1) Molecular Systems Department, P.O. BOX 4, West Point, PA 19486
(2) Molecular Systems Department, P.O. BOX 2000, Rahway, NJ 07065
(3) Basic Research Systems, P.O. BOX 4, West Point, PA 19486
(4) Basic Research Systems, P.O. BOX 2000, Rahway, NJ 07065
(5) Medicinal Chemistry Department,  P.O. BOX 4, West Point, PA 19486

Motivated by the need to augment Merck’s in-house small molecule collection, web-based tools for designing, enumerating, optimizing and tracking compound libraries have been developed. The path leading to the current version of this virtual library tool kit (VLTK) is discussed in context of the (then) available commercial offerings and the constraints and requirements imposed by the end users. Though the effort was initiated to simplify the tasks of designing novel, drug-like and diverse compound libraries containing between 2K-10K unique entities, it has also evolved into a powerful tool for outsourcing syntheses as well as lead identification and optimization. The web tool includes components that select reagents, analyze synthons, identify backup reagents, enumerate libraries, calculate properties, optimize libraries and finally track the synthesized compounds through biological assays. In addition to accommodating project specific designs and virtual 3D library scanning, the application includes tools for parallel synthesis, laboratory automation and compound registration.
To whom correspondence should be addressed.

Search-and-query Information System for the Study and Discovery of Novel Agents in the Treatment of Cancer

David Covell, National Cancer Institute, Building 1052, Rm 236, Frederick, MD 21702-1201, USA

The National Cancer Institute has maintained a panel of immortalized tumor cell lines since 1990 for the purpose of screening chemical agents as candidates in the search for more effective cancer treatments. During these past 25 years nearly 80,000 small synthetic compounds and an equal number of natural product extracts have been assayed in the NCI’s tumor screen. In parallel with this screening effort, the NCI has maintained a follow-up protocol comprised of secondary testing of active compounds in hollow-fiber and xenograft models. Parallel measurements of gene expressions within the NCI’s tumor cell panel have complemented this data as well as the development of nearly a dozen molecular target assays screened against a panel of ~200,000 small molecules. The data generated in these screens has been the subject of efforts to devise informatic-based methods for data mining. The product of this effort is embodied within the publicly accessible web tool at the url ‘spheroid.ncifcrf.gov’. The utilities within this web site represent a search-and-query information system for the study and discovery of novel agents in the treatment of cancer. The functionalities within this web utility allow interactions with a wide range of public databases and the NCI’s screening data. Presentation and discussion of these utilities will be made in the context of recent drug discovery explorations.

PubChem

Steve Bryant, NCBI

PubChem is a new online information resource from NCBI. The system provides information on the biological properties and activities of chemical substances. Following the sequence-deposition model followed by GenBank, PubChem's content is derived from user depositions of chemical structure and
bioassay data, including data from NIH's Molecular Libraries initiative. The retrieval system supports searches based on chemical names and chemical structure, as well as searches based on bioassay descriptions and activity information. It furthermore provides links to depositor sites, for further information, as well as links to other NCBI resources such as the PubMed literature database and Entrez's protein 3D structure database.

ZINC web services - providing 3D structures of purchasable compounds for virtual screening to humans and machines

John Irwin, Pharmaceutical Chemistry, UCSF, 1700 4th St, Suite 501D, San Francisco CA 94143-2550 USA

Despite the successes of virtual screening, and its growing use, there remain many barriers to entry for non-specialists wishing to use this technology. We created the ZINC database, a free collection of commercially available compounds for virtual screening to lower one of these barriers. We made ZINC more flexible and adaptive by creating web services. Molecules matching specific criteria, including chemical structures, may be searched, often in less than a minute. Results of datasbase searches may be reviewed in a web browser, the 3D structure of molecules may be viewed in a Jmol applet, and structures may be downloaded individually or en masse in popular formats. Because there will always be molecules that are not in ZINC, we allow users to upload and process their own molecules using the same protocols we use to prepare the database. The ZINC webserver can also handle queries in machine readable form using a well defined ontology.

BASEL SESSION

Open Archives as a Route for the Capture, Dissemination and Access to Chemical Information

Simon J. Coles, School of Chemistry, University of Southampton, Highfield, Southampton, Hampshire, SO17 1BJ, UK

Modern advances in high throughput synthesis, scientific analytical instrumentation and data analysis and mining techniques are presenting increasingly big challenges for chemical information management and discovery. Consequently, the conventional process of peer review of journal articles as the primary route for the dissemination of scientific data is unable to keep apace with these high rates of generation and is hindering the passage of this data to the public domain. The architecture and philosophy of the Open Archive presents a solution to both the data management and publication problems.

     Recent work undertaken by the eBank-UK project (http://www.ukoln.ac.uk/projects/ebank-uk/) has been addressing the issue of dissemination of scientific data and uses the philosophy of the Open Archive Initiative (OAI) to solve this problem, whilst the R4L project (http://r4l.eprints.org) uses the same approach for laboratory data management. The UK National Crystallography Service (NCS) (http://www.ncs.chem.soton.ac.uk/) has developed an Open Archive infrastructure for crystal structure data (http://ecrystals.chem.soton.ac.uk) as an exemplar of this methodology.

    All the data generated during the course of the crystal structure determination experiment is seamlessly or automatically captured, time-stamped for priority assertion purposes and deposited in a laboratory management repository. A report generation tool is then employed to collate all experimental information in the laboratory repository, based on a particular compound. This report is utilised to prepare a journal article, based on the experimental data, and both write ups are subsequently deposited in an Institutional Repository. The Institutional Repository publicises its data content to the internet through Open Archive Initiative (OAI) protocols, which allows aggregator services to harvest pertinent metadata. The aggregator search and discovery tools then provide seamless and unhindered access to the scientific reports and their underlying data, thus maximising efficient sharing of experimental chemical information.

Investigating chemical trends in the context of ligand-protein complexes by using on-line data analysis directly on the web

Dimitris Dimitropoulos, EMBL Outstation - Hinxton, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD, United Kingdom

A prebuild relational data-warehouse with a rich set of relationships for the PDB and the PDB ligands, is the perfect environment for evaluating interesting research questions that may potentially reveal links between ligand chemistry, and the protein environment characteristics. In the MSD search database several common functional groups have been identified for ligands and associated on the atom level to the occurrences of the bound molecules in PDB entries using a consistent nomenclature. These are used as a starting point in order to explore the chemistry relationships to binding site information, secondary structure, and protein classification. As an example we will demonstrate how the MSD-mine tool for on-line data analysis and mining over the web, can be used to examine potential preference of functional fragment distribution towards particular SCOP domains, and in a separate example the contribution of different fragment areas in the binding site activity. The MSD-mine tool and the example scenarios are accessible from http://www.ebi.ac.uk/msdmine.

Identification of biological units in protein crystals

Eugene Krissinel & Kim Henrick, European Bioinformatics Institute, Hinxton, Cambridge, CB10 1SD, UK

PDB entries of protein structures solved by means of X-ray diffraction on protein crystals represent asymmetric units (ASU) of the crystals. In most instances, ASU may be chosen in many different ways and they do not necessarily coincide with the biological units, or stable protein assemblies that perform certain physiological functions. It is reasonable to expect that protein assemblies merge, rather than transform, during the crystallisation, therefore protein crystals do carry rather valuable data on the composition and geometry of biological units. Given that nearly 80% of PDB entries are obtained by means of protein crystallography and that direct experimental identification of assembly structure is difficult, detection of biological units in protein crystals is of considerable practical interest.

We propose a new approach to the problem from general principles of chemical thermodynamics, which is different from previous attempts [1,2] based on scoring of individual protein interfaces in crystal. We perform an exhaustive graph-theoretical search of all assemblies that are possible in a given crystal, and leave only those that appear to be thermodynamically stable. The stability estimate is based on the consideration of protein affinity and entropy change upon dissociation. Applied to PDB entries with oligomeric states known from the literature, our method gives 89% of correct predictions, which is higher than previously reported [2].

The method is implemented as a publicly available web server (http://www.ebi.ac.uk/msd-srv/prot_int/cgi-bin/piserver), which provides the assembly-related data for all PDB entries of structures solved by X-ray diffraction. The server can take PDB and mmCIF-formatted coordinate files for upload and calculate protein assemblies in real time (a few minutes in most instances). Detail, on-residue level, data on protein interactions, solvation energies, surface areas, hydrogen bonds and salt bridges are provided on output. Probable dissociation patterns of stable assemblies are also calculated. The calculated assemblies and individual crystal contacts (interfaces) may be visualised using the Rasmol software. The server includes a search facility for the identification of structurally equivalent protein interfaces in the PDB archive.

[1] Henrick, K.; Thornton, J. Thrends Biochem. Sci., 1998, 23, 358.
[2] Ponstingl, H.; Kabir, T.; Thornton, J. J. Appl. Cryst. 2003, 36, 1116.

SWISS-MODEL Server and Repository: Web based resources for comparative protein structure modeling and their application in drug discovery

Jürgen Kopp, Lorenza Bordoli, Konstantin Arnold, Markus Meuwly, Vincent Zoete, Hólmfríður B. Þorsteinsdóttir, and Torsten Schwede, University of Basel (Switzerland) & Swiss Institute of Bioinformatics

One of the bottlenecks of structure-based drug design is the availability of experimentally determined protein structures. Today, the number of structurally characterized proteins is about two orders of magnitude smaller than the number of known protein sequences, i.e. no direct experimental structural information is available for the vast majority of protein sequences. Theoretical methods for protein structure prediction are aiming to bridge this structure knowledge gap. As shown during the biannual CASP experiments, homology modeling is the only computational approach, that can generate accurate three-dimensional models for a protein for successful application in structure based drug development. The SWISS-MODEL Server and Repository have been developed to provide instant web-based access to annotated models generated by automated homology modeling, bridging the gap between sequence and structure databases.

Validation of homology models for drug discovery applications is a crucial aspect, and one important question is how errors and inaccuracies of the homology models affect the molecular modeling of protein-ligand interactions. We used a MM-GBSA approach to compute the binding free energy of interaction of 16 HIV-1 protease inhibitor complexes in experimental and model structures. Using this system, we can introduce systematic errors in the protein model to simulate the typical inaccuracies that occur during homology modeling to quantify the effect on ligand binding affinity and ranking of inhibitors.

References:
Schwede T, Kopp J, Guex N, and Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research 31, 3381-338.
Kopp J, and Schwede T (2004). The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Research 32 , D230-D234.
Contact: Torsten Schwede

The Representation of Chemical Structures and its Application to Property Prediction

Johann Gasteiger, Computer-Chemie-Centrum, Universität Erlangen-Nürnberg
D-91052 Erlangen, Germany

The relationships between the structure of a chemical compound and many of its physical, chemical, or biological properties are too complex to be calculated from first principles. This is particularly true for the biological activity of a compound.  In this situation an indirect approach has to be taken.[1]  First, chemical descriptors have to be calculated for the molecular structure. Then, a relationship between these structure descriptors and the property to be predicted has to be established by inductive learning methods such as statistical or pattern recognition methods or neural networks. Methods for calculating structure descriptors available on the internet will be presented. Furthermore, program packages for data analysis and data mining that can be accessed on the web will be indicated. Of crucial importance for property modeling is the availability of data. Fortunately, increasingly, data become available on the internet. Some applications in modeling properties such as solubility or toxicity will be presented.

[1]  Chemoinformatics – A Textbook , J. Gasteiger, T. Engel (Editors), Wiley-VCH,
       Weinheim, 2003.

Barry Hardy
eCheminfo Community of Practice Manager
Douglas Connect, Switzerland

July 18, 2005

Protein Folding and Dynamics

After decades of largely independent experimental and theoretical work, the field of protein folding is entering a mature age in which the two are converging. Experimental techniques have become sophisticated enough to probe the folding of small, fast-folding proteins and protein elements, while computational power and algorithms have reached a level at which simulating these events is tractable. The central goal our eCheminfo "Protein Folding and Dynamics" program is to bring together researchers working on both theoretical and experimental fronts of the protein folding field, and have them present recent cutting-edge research results.

We will be holding the “Protein Folding and Dynamics" InterAction Meeting session in Basel, Switzerland on 9 November 2005.  The purpose of the meeting is to bring together world-class researchers to present and discuss recent and new approaches and results in research areas relevant to both basic protein research and applications relevant to Alzheimer’s, Huntington’s Disease, and other diseases. The emphasis of the meeting activity is on communication and open discussion, which we hope will lead to new ideas and collaborations towards progress and innovation in the areas discussed.  A significant amount of time at the meeting will be devoted to question time and panel and group discussions towards this goal.

A description of the session and invited speaker presentations follows:

eCheminfo InterAction Meeting Session, Basel, 9 November 2005

Protein Folding and Dynamics
chaired by chaired by Wilfred van Gunsteren (ETH-Zurich)
eCheminfo and InnovationWell 2005 InterAction Meetings, 9-10 November 2005, Basel, Switzerland
Program Updates loaded in the Program Areas on http://echeminfo.com/ and http://innovationwell.net/

Invited Speakers and Discussion Leaders:

Jeremy Smith (University of Heidelberg), Wolfgang Wenzel (University of Karslruhe), Thomas Kiefhaber (University of Basel), Xavier Daura (University of Barcelona), Nikolay V. Dokholyan (University of North Carolina) and Michele Vendruscolo (University of Cambridge)


Presentation Abstracts:

Dynamics of Protein Binding, Reaction and Structural Change
Jeremy C. Smith, Computational Molecular Biophysics, Faculties of Biological Science and Physics/Astronomy, Heidelberg University, Germany

Computer simulation results on dynamical effects influencing ligand binding, reactions and the mechanics of large-scale conformational change in proteins will be discussed.  Among the questions to be examined are the thermodynamic consequences of vibrational changes on ligand binding, the protein glass transition and function, proton transfer reactions in the light-driven proton pump protein, bacteriorhodopsin, and the mechanics of the power stroke of muscle contraction.


Aspects of beta-peptide folding from molecular-dynamics simulation

Xavier Daura, Catalan Institution for Research and Advanced Studies (ICREA) and Institute of Biotechnology and Biomedicine (IBB), Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), Spain

Due mostly to work from the groups of D. Seebach at ETH Zürich and S. H. Gellman at University of Wisconsin, there is now considerable knowledge on the chemistry and "biology" –the possible biomedical and biotechnological applications– of beta-peptides. Since 1997, stimulated by D. Seebach and co-workers, we have been working on several aspects of beta-peptide structure and dynamics, including folding thermodynamics and kinetics. My presentation will be centred around two such aspects, which we have been recently investigating. The first one refers to the accessible conformational spaces of two beta-peptides in methanol at different temperatures, which we have analysed in terms of network theory. Here, the populated conformational states are determined by clustering peptide structures sampled at regular time intervals during the simulation. Each conformational state represents, thereafter, a node in the graph –network–. Links between nodes correspond to bidirectional transitions between conformational states –clusters– sampled during the simulation. Comparison of the resulting graphs to theoretical models gives us information on the properties of the conformational free-enthalpy landscape of the peptides. The second one refers to the energetics of one of these two peptides, which we have analysed using classical-thermodynamics formulae that relate free-enthalpy and entropy differences over a temperature range to enthalpies and heat capacities at constant pressure. Two of the conclusions from this work were unexpected.


All-atom protein folding with stochastic optimization methods

A. Schug , A. Verma and W. Wenzel, Forschungszentrum Karlsruhe, Institut für Nanotechnologie, Karlsruhe, Germany

The prediction of protein tertiary structure, in particular based on sequence information alone, remains one of the outstanding problems in biophysical chemistry. We have recently developed an all-atom free energy forcefield (PFF01) which implements a minimal thermodynamic model based on physical interactions and an implict solvent model. We could demonstrate that PFF01 stabilizes the native conformation of several helical proteins as the global optimum of its free energy surface. In addition we were able to reproducibly fold several helical proteins, ranging 20-60 amino acids in size from random starting conditions. We used several stochastic optimization methods: the stochastic tunneling method, an adapted version of parallel tempering, basin hopping techniques and distributed evolutionary optimization strategies. We will discuss advantages and limitations with respect to further improvements of this approach to in-silico all-atom protein structure prediction.


Structure determination of native and non-native protein conformations using NMR-derived restraints

Michele Vendruscolo, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK

In recent years increasingly detailed information about the structures and dynamics of protein molecules has been obtained by innovative applications of NMR techniques and of theoretical methods, in particular molecular dynamics simulations. I will discuss how such approaches can be combined by incorporating a wide range of different types of experimental data as restraints in computer simulations to provide unprecedented detail about the ensembles of structures that describe proteins in a wide variety of states from the native structure to highly unfolded species. This strategy has provided, in particular, new insights into the mechanism by which proteins are able to fold into their native states, or by which they fail to do so and give rise to harmful aggregates that are associated with a wide range of debilitating human diseases.


Simple yet Predictive Protein Models

Nikolay V. Dokholyan, University of North Carolina at Chapel Hill, School of Medicine, Campus Box 7260, Chapel Hill, NC 27599, USA

The traditional approach to computational biophysics studies of molecular systems is brute force molecular dynamics simulations under conditions of interest. The disadvantages of this traditional approach are that the time and length scales accessible to computer simulations often do not reach biologically-relevant scales. An alternative approach, which we call intuitive modeling, is hypothesis-driven and is based on tailoring simplified protein models to the systems of interest. Using intuitive modeling, the length and time scales that are achievable using simplified protein models by far exceed those of the traditional molecular dynamics simulations. We will describe several recent studies that signify the predictive power of simplified protein models within the intuitive modeling approach.


Protein Dynamics Measured by Triplet-Triplet Energy Transfer

Thomas Kiefhaber, Biozentrum der Universität Basel, Division of Biophysical Chemistry
Klingelbergstr. 70, CH-4056 Basel, Switzerland

The rate at which a protein can explore conformational space during folding is limited by intrachain diffusion processes. The maximum rate for protein folding can not exceed the rates of intramolecular contact formation [1]. To understand the dynamics of unfolded polypeptide chains we studied contact formation between individual amino acid residues using diffusion controlled triplet-triplet energy transfer (TTET) [2]. We attached xanthone as triplet donor and naphtylalanine as triplet acceptor at  the ends of  polypeptide chains with different sequence and varied the distance between donor and acceptor from 3 to 60 amino acids. We observed single exponential kinetics for end-to-end diffusion in all peptides.  In flexible poly(Gly-Ser) chains the time constant for contact formation reaches an upper limit of about 5 ns, which sets the speed limit for protein folding. This value is nearly independent of chain length for short donor-acceptor distances (N<8; N=number of peptide bonds between donor and acceptor). In the limit of long chains (N>20) the rate of end-to-end diffusion scales with N^(-1.7). We found only little effect of the amino acid sequence on local chain dynamics. In host-guest  peptides the stiffest side chain (Pro)  showed only about 8-fold slower chain dynamics compared to the most flexible amino acid (Gly) [3].

During protein folding most interactions are formed between amino acids in the interior of the polypeptide chain. To test for differences in the dynamics of intrachain diffusion compared to end-to-end diffusion we studied contact formation in a series of peptides that had either one end or both ends extended beyond the position of the triplet donor/acceptor. We observed significantly decreased contact rates with increasing mass/surface of the additional tails until a limiting value is reached.

To compare the results obtained from homo-polypetides with natural protein sequences we measured dynamics in various loops from carp-parvalbumin and in the GB1 hairpin [4]. The results are in  agreement with the dynamics expected from the host-guest  peptides. Interestingly, intrachain diffusion in the natural sequences showed significant activation energies, which were similar to activation energies found for protein folding reactions (15-20 kJ/mol).  Studies on helical peptides further revealed that  TTET can be used to measure unfolding dynamics of protein secondary structures.

References: 
1. Bieri, O., Kiefhaber, T., Biol. Chem. 380 (1999) 923.
2. Bieri, O., Wirz, J., Hellrung, B., Schutkowski, M., Drewello, M., Kiefhaber, T., Proc.
Natl. Acad. Sci. USA 96 (1999) 9597.
3. Krieger, F., Fierz, B., Bieri, O., Drewello, M., Kiefhaber, T., J. Mol. Biol. 332 (2003)
265.
4. Krieger, F., Fierz, B., Axthelm, F., Joder, K., Meyer, D., Kiefhaber, T., Chemical
Physics (2004) in press.

Barry Hardy
Community of Practice Manager
Douglas Connect

July 14, 2005

Protein Folding, Misfolding & Aggregation: Applications to Disease (Alzheimer’s, Huntington’s, Renal Failure)

Approaches to medicine are rapidly changing as we begin to comprehend human disease at the most fundamental molecular level. Much of this change is heralded by a more quantitative and mechanistic understanding of the alterations of molecular structure and dynamics that produce disease. Recent years have brought a dramatic increase in the number of known associations between human disease and abnormalities in protein dynamics and structure. In particular, the number of diseases known to be associated with protein aggregation has increased several-fold. Since protein structure and dynamics are intimately related to protein cellular function, abnormalities in protein folding dynamics and structural stability often adversely affect cell life. Understanding protein folding, misfolding and aggregation will be vital to understanding human diseases, ranging from various forms of cancer to neurodegenerative diseases, and will facilitate the development of therapeutic strategies to combat these diseases.

We are holding an InterAction Meeting session at Bryn Mawr College, Philadelphia on October 12th on "Protein Folding, Misfolding & Aggregation: Applications to Disease".  The purpose of the meeting is to bring together world-class researchers working on both theoretical and experimental fronts of the protein folding field, and have them present and discuss recent and new results in cutting-edge research areas relevant to Alzheimer’s, Huntington’s Disease, other neurodegenerative diseases and Renal Failure. The emphasis of the meeting activity is on communication and open discussion, which we hope will lead to new ideas and collaborations towards progress and innovation in the disease areas discussed.  A significant amount of time at the meeting will be devoted to question time and panel and group discussions towards this goal.

A description of the session and invited speaker presentations follows:

eCheminfo InterAction Meeting Session, Philadelphia, 12 October 2005
Protein Folding, Misfolding & Aggregation: Applications to Disease
chaired by Nikolay V. Dokholyan (University of North Carolina at Chapel Hill),
eCheminfo and InnovationWell Autumn 2005 InterAction Meetings, 11-12 October 2005, Philadelphia, USA
Program Updates loaded in the Program Areas on http://echeminfo.com/ and http://innovationwell.net/

Invited Speakers and Discussion Leaders:

David Teplow (David Geffen School of Medicine at UCLA), Ron Wetzel (University of Tenessee Medical Center), Michael Thorpe (Arizona State University), Feng Ding (University of North Carolina), Andrew Miranker (Yale University)

Presentation Abstracts:

Amyloid beta-protein oligomerization and Alzheimer’s disease
David B. Teplow, Department of Neurology, David Geffen School of Medicine at UCLA, 635
Charles E. Young Drive South (Room 445), Los Angeles, CA 90095-7334, USA

A seminal etiologic component of many neurodegenerative diseases is the abnormal folding and assembly of proteins. This process produces a variety of monomeric, oligomeric, and polymeric structures. In Alzheimer’s disease (AD), work by anatomists in the 19th century first implicated amyloid fibrils in disease causation. Amyloid fibrils are protein homopolymers with large aspect ratios, diameters of ca.10 nm, and common core structural organization. Amyloid fibrils also form in other neurodegenerative diseases, including the transmissible spongiform encephalopathies, Parkinson’s disease, amyotrophic lateral sclerosis, and familial amyloid polyneuropathy. The wide occurrence and obvious clinical linkage of amyloid formation to neurodegeneration has stimulated intense study of amyloidogenesis. The amyloid hypothesis, which argues the primacy of amyloid fibrils in the neuropathogenesis of AD, was one of the first results of these investigations. However, a broad and increasingly compelling body of recent work now supports a revision of the hypothesis. Specifically, the primacy of fibrils in AD pathogenesis has been supplanted by the primacy of low-order oligomers.

In AD, fibrils are formed by the amyloid beta-protein (Abeta). Understanding, in molecular detail, the folding and oligomerization of the Abeta monomer has been complicated by the facts that the peptide has no stable native fold, displays a complex folding topography, and populates biologically-relevant conformational states transitorily. Nevertheless, new experimental and computational approaches have provided the means to identify and characterize novel assembly intermediates, including short, flexible, fibril-like polymers termed “protofibrils” and small pentamer/hexamer units termed “paranuclei.”

Protofibrils are neurotoxic and their formation appears to be a general feature of the assembly of many different amyloidogenic proteins. Paranuclei-like assemblies have been found in AD patients and may be the proximate neurotoxins in AD. I will discuss recent results of studies of Abeta folding and assembly and the implications for understanding and treating AD.

The assembly and structure of amyloid-like polyglutamine aggregates associated with Huntington’s Disease
Ronald Wetzel, University of Tenessee Medical Center

In Huntington’s disease (HD) and seven other expanded CAG repeat diseases, the mutational increase in length of a polyglutamine (polyGln) segment of various disease-specific proteins above a pathological repeat length of about 35 residues is associated with a sharp increase in disease risk.  Additional lengthening of the polyglutamine leads to earlier disease onset.  Since these polyglutamine disease proteins vary in size, structure, sub-cellular localization and function, the expanded polyglutamine sequence itself must be the driving force of disease.  To arrive at the basis for polyglutamine pathogenesis, we are studying how repeat length influences the physical properties of polyglutamine sequences, and in particular their abilities to form amyloid-like aggregates similar to those found in HD neurons.

Cells treated with nuclear-targeted aggregates of polyglutamine peptides are very effectively killed in an apoptosis-related mechanism.  Cells pretreated with a peptide-based elongation inhibitor are protected.  Small aggregation foci can be identified in 10-20 year old archival HD brain tissue using a staining procedure based on aggregate elongation.  All this is consistent with toxicity mechanisms depending on the ability of polyglutamine sequences to aggregate.  Learning more about the details of polyglutamine folding and aggregation is therefore critically important.

The solution conformation of monomeric polyglutamine appears to depend little on repeat length, suggesting that a repeat length dependent conformational change is not responsible for toxicity.  In contrast, aggregation kinetics are sharply dependent on repeat length.  Polyglutamine makes amyloid-like aggregates by a classical nucleation-dependent polymerization mechanism.  Surprisingly, we found the critical nucleus to be one, suggesting that the energetically unfavorable nucleation event in this system is not oligomerization, but rather folding of the monomer into an aggregation-competent structure.  Longer polyGln sequences aggregate more efficiently because their nucleation equilibrium constant is more favorable.  The nucleation equilibrium constant for a Q47 repeat sequence is in the range of 10-9, illustrating the unfavorable nature of nucleus formation.  The interplay between nucleus formation and subsequent elongation events is illustrated by the ability of short polyGln peptides to enhance the overall nucleation and aggregation of a long polyGln sequence.  This underscores the potential importance of the entire polyglutamine protein population in controlling the cell’s susceptibility to an expanded polyGln protein.

It should now be feasible to begin to probe how additional features of the various disease proteins and their environments produce disease-specific effects.  Other examples of important variables now being studied include the polyGln flanking sequences of huntingtin, and the presence of certain molecular chaperones in the cellular environment.  It should also be possible to develop small molecule inhibitors of polyglutamine aggregation as potential therapeutics.

Catalytic origins of protein misfolding in end-stage renal failure

Andrew Miranker, Dept. of Molecular Biophysics and Biochemistry Office, Yale University Lab, 266 Whitney Avenue / Bass 318 PO Box 208114, New Haven, CT 06520-8114, USA

Amyloid fibers are long, unbranched and insoluble homo-assemblies of proteins. The self-assembly of such structures occurs in a number of human diseases such as Alzheimer's, as part of biological function such as in melanin deposition, and as a scaffold for design as in the formation of conductive wires. The process of fiber formation is complex with nucleation dependent kinetics giving rise to cytotoxic intermediates resulting in a product which is macroscopic. These properties are the result, in part, of a transient and heterogeneous assembly mechanism making structural insight particularly challenging. b-2-microglobulin (b2m) is the conserved, 99 amino acid globular protein required for the correct folding and cell surface expression of class I major histocompatability complex. In patients with end-stage renal disease treated by hemodialysis, b2m undergoes transitions resulting in its deposition as amyloid principally in the liver and joint spaces. Our recent analyses of b2m amyloid formation have enabled us to identify the existence of a monomeric and native-like intermediate on the pathway of fiber formation. This state, is catalytically accessed by the presence of transition metal cation. This intermediate rapidly assembles into discrete oligomeric states which display little additional oligomerization on the timescale of their own formation (<1hr). Amyloid fiber formation progresses from these intermediate states but on much longer timescales. The native-like structure and discrete oligomeric size of these amyloid intermediates suggests that this protein forms fibers by structural domain swapping. As transition metal cation effects are reported in many other amyloidoses, e.g. prion, Parkinson's, and Alzheimer's, elucidation of the mechanism of b2m amyloid formation enables us to define general mechanisms for divalent ion associated amyloidosis.

Direct observation of protein folding, misfolding and prion-like conformational infectivity
Feng Ding, Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 303 Mary Ellen Jones, CB#7260, Chapel Hill, NC 27599, USA
   

Protein conformational transition from alpha-helices to beta-sheets precedes aggregation of proteins implicated in many diseases, including Alzheimer’s and prion diseases. Direct characterization of such transition is often hindered by the complicated nature of the interaction network among amino acids. A recently engineered small protein-like peptide with a simple amino acid composition features a temperature-driven alpha-helix to beta-sheets conformational change. Here, we study the conformational transition of this peptide by molecular dynamics simulations. We find a critical temperature, below which the peptide folds into an alpha-helical coiled-coil state, and above which the peptide misfolds into beta-rich structures with a high propensity to aggregate. The structures adopted by this peptide during low temperature simulations have a backbone root mean square deviation less than 2 Å from the crystal structure. At high temperatures, this peptide adopts an amyloid-like structure, which is mainly comprised of coiled anti-parallel beta-sheets with the cross-beta signature of amyloid fibrils. Strikingly, we directly observe “infective” conformational conversions, where an alpha-helix is converted into a beta-strand by proximate stable beta-sheets with exposed hydrophobic surfaces and unsaturated hydrogen bonds. Our study suggests a possible molecular mechanism of the seeded aggregation process as proposed by Prusiner for the infectivity of prions.

Flexibility and Mobility in Biomolecules

M.F. Thorpe, B.M. Hespenheide, S. Menor and S. Wells, Bateman Physical Sciences PSF 359
Arizona State University, Tempe, AZ 85287-1504, USA

We present a novel approach to the calculation of flexibility and mobility in proteins, protein complexes and other large macromolecular complexes like virus capsids. Rather than using conventional molecular dynamics, we use the constraint approach of Lagrange, incorporating covalent bonds, hydrogen bonds, and tethers for hydrophobic interactions. The rigid clusters, including the core, are identified as well as the flexible joints between them. This is used as the basis for dynamics, using Monte Carlo approaches that maintain all the original constraints, as well as van der Waals excluded volumes.

In our original work [1, 2], we focused on ring closure and added the side groups later. This was successful in exploring the available conformational space and also in exploring directed trajectories between known distinct protein structures.

In more recent work, we have used ghost templates attached to the rigid regions to guide a protein through the allowed conformational space. The generation of a new protein conformation requires about 100 millsecs CPU time on a single processor [3].

We show that such techniques can be used on a single X-ray crystallographic structure to generate an ensemble of structures remarkably similar to those observed in NMR. We also show how this approach can be used to generate multiple protein complexes for use in ligand docking studies, as well as exploring the allowed conformations of protein-ligand complexes. We discuss applications to virtual screening and the drug discovery process.

Acknowledgement: Work supported by NSF and NIH.

References:
[1] Ming Lei, Leslie A. Kuhn, Maria I. Zavodszky and M.F. Thorpe Sampling Protein Conformations and Pathways, Journal of Computational Chemistry 25, 1133–1148 (2004).
[2] Maria I. Zavodszky, Ming Lei, M.F. Thorpe, Anthony R. Day and Leslie A. Kuhn Modeling Correlated Main-Chain Motions in Proteins for Flexible Molecular Recognition, Proteins: Structure, Function and Bioinformatics 57, 243–261 (2004).
[3] Stephen Wells, Brandon Hespenheide, Scott Menor and M.F. Thorpe Constrained Geometrical Simulation of Diffusive Motions in Proteins (to be published in Physical Biology).

Barry Hardy
eCheminfo Community of Practice Manager
Douglas Connect

July 12, 2005

eCheminfo European Autumn 2005 InterAction Meeting

The eCheminfo European Autumn 2005 InterAction Meeting will be taking place at the Swissotel L’entrée Conference Center, Basel, Switzerland, Nov 9-10.  Program information and registration is available through the eCheminfo website at http://echeminfo.com/

The theme of the meeting is the application of cheminformatics and chemical modelling to drug discovery and will include the following sessions:

Virtual Screening, Docking & Scoring, chaired by Miklos Vargyas (ChemAxon); Web-based Services in Drug Design, chaired by Kim Henrick (European Bioinformatics Institute); Computational Biochemistry, chaired by Alessandro Curioni (IBM Zurich); Applications of Machine Learning & Graph Mining in Drug Discovery, chaired by Stefan Kramer (Technische Universitaet Muenchen); Biosensors & Nanofluidics, Nick Quirke (Imperial College London); Protein Folding and Dynamics, chaired by Wilfred van Gunsteren (ETH-Zurich)

Invited Speakers include:
Graham Richards (University of Oxford), Xavier Barril (Vernalis), Amedeo Caflisch (ETH-Zurich), David Morley (Enspiral Discovery Ltd), Didier Rognan (University of Strasbourg), Dimitris Dimitropoulos (European Bioinformatics Institute), Johann Gasteiger (Universitaet Erlangen-Nuernberg), Simon Coles (University of Southampton), Eugene Krissinel (European Bioinformatics Institute), Torsten Schwede (University of Basel), Paul Tavan (University of Munich), Ursula Roethlisberger (Swiss Federal Institute of Technology, Lausanne), Alessandro Curioni (IBM Zurich), Ian Williams (University of Bath), Gerald Monard (Universite Henri Poincare – Nancy), Ken Merz (QuantumBio), Nick Quirke (Imperial College London), Richard Gilbert (E2v Technologies), Andrew De Mello (Imperial College London), Jens Walther (ETH-Zurich), Christoph Helma (University of Freiburg), Peter Willett (University of Sheffield), Joost N. Kok (Leiden University), Gisbert Schneider (Johann Wolfgang Goethe-University), Michael Berthold (University of Konstanz), Jeremy Smith (University of Heidelberg), Wolfgang Wenzel (University of Karslruhe), Thomas Kiefhaber (University of Basel), Xavier Daura (University of Barcelona), Nikolay V. Dokholyan (University of North Carolina), Michele Vendruscolo (University of Cambridge)

The eCheminfo meetings will have exhibitor tables for software demos and evening poster sessions; posters will also be available for viewing through the website.  Posters can be on any informatics or modeling topic of relevance to drug discovery. Those who cannot make the meetings are also able to register to access all presentations, posters and discussions through the eCheminfo website. Registrants for the European meeting will also be able to access the full proceedings with audio of the equivalent US meeting being held in Philadelphia.

Poster Abstracts (ca. 300 words) should be sent to eCheminfo at douglasconnect.com

The InnovationWell European community of practice Autumn meeting will be taking place at the same location and on the same dates as the eCheminfo European meeting.  This meeting will be covering semantic web applications in drug discovery and development, life science intellectual property management and valuation; knowledge management and transfer in R&D and manufacturing, clinical trial productivity, drug safety knowledge management and predictive toxicology.  All eCheminfo registrants will also have access to the InnovationWell meeting activities. (See http://innovationwell.net/ for more details).

Please register early for the meetings as the number of places are limited.  You can register for the meeting on the website or contact Nicki Douglas (nicki.douglas at douglasconnect.com, +41 61 851 0461) to reserve your place.

Barry Hardy
Community of Practice Manager
Douglas Connect

eCheminfo US Autumn 2005 InterAction Meeting

The eCheminfo US Autumn 2005 InterAction Meeting will be taking place at Bryn Mawr College, Philadelphia, US, 11-12 October.  Program information and registration is available through the eCheminfo website at http://echeminfo.com/

The theme of the meeting is the application of cheminformatics and chemical modelling to drug discovery and will include the following sessions:

Virtual Screening, Docking & Scoring, chaired by Max Cummings (Johnson & Johnson); Web-based Services in Drug Design, chaired by Marc Nicklaus, (National Institutes of Health); Protein Folding, Misfolding & Aggregation: Applications to Disease, chaired by Nikolay V. Dokholyan (University of North Carolina); New Developments in Biophysical Applications of Quantum Mechanics, chaired by Ken Merz/Lance Westerhoff (QuantumBio); Simulation of Membranes & Ion Channels, co-chaired by Richard Pastor (FDA) & Michael Klein (University of Pennsylvania)

Invited Speakers include:
Emanuele Perola (Vertex), Mark McGann (Openeye), John Irwin (UCSF), Renee DesJarlais (Johnson & Johnson), Willem Nissink (Cambridge Crystallographic Data Centre), Brad Feuston (Merck), Brett Tounge (Johnson & Johnson), Steve Bryant (NCBI), David Covell (NCI), Andrew Miranker (Yale University), David Teplow (David Geffen School of Medicine at UCLA), Ron Wetzel (University of Tenessee Medical Center), Michael Thorpe (Arizona State University), Feng Ding (University of North Carolina), Mike Pitman (IBM), Jeff Klauda (NIH), Emad Tajkhorshid (Beckman Institute, University of Illinois at Urbana-Champaign), Richard Pastor (FDA), Preston Moore (USIP), Jian Li (Johnson & Johnson), Martin Peters (Penn State), Darrin York (University of Minnesota)

The eCheminfo meetings will have exhibitor tables for software demos and evening poster sessions; posters will also be available for viewing through the website.  Posters can be on any informatics or modeling topic of relevance to drug discovery. Those who cannot make the meetings are also able to register to access all presentations, posters and discussions through the eCheminfo website. Registrants for the US meeting will also be able to access the full proceedings with audio of the equivalent European meeting being held in Basel, Switzerland.

Poster Abstracts (ca. 300 words) should be sent to eCheminfo at douglasconnect.com

The InnovationWell US community of practice Autumn meeting will be taking place at the same location and on the same dates as the eCheminfo US meeting.  This meeting will be covering semantic web applications in drug discovery, personalised medicine, knowledge management and transfer in R&D, clinical trial productivity, drug safety knowledge management and predictive toxicology.  All eCheminfo registrants will also have access to the InnovationWell meeting activities. (See http://innovationwell.net/ for more details).

Please register early for the meetings as the number of places are limited.  You can register for the meeting on the website or contact Nicki Douglas (nicki.douglas at douglasconnect.com, +41 61 851 0461) to reserve your place.

Barry Hardy
Community of Practice Manager
Douglas Connect

July 04, 2005

Making Web-based Services work for Drug Discovery in Industry and Academia

Pharmaceutical research is under challenge to improve the choice, quality and safety of lead candidates. There is a clear need for an open discussion and an awareness of the requirements for a much more complex knowledge management and knowledge transfer between academic, government and commercial interests. The semantic web has the potential to make significant contributions to the drug discovery of the future but is at this time at an early development stage and there are only a few public tools for the data mining and sharing of chemical information.

Just a few years ago, the only imaginable way of doing in silico drug design - or, indeed, any cheminformatics research - was to use in-house and commercial software and databases. New developments in Web services however are offering today’s researchers additional resources. Although cheminformatics admittedly lags far behind bioinformatics (where an enormous wealth of data and software is literally a click away), we are beginning to see some chemical resources in open access.

A goal for this session on "Web-based Services in Drug Design" is to present some of the possibilities of web-based tools and data and to lead into discussions on how can web services work for both the academic world and industry, while maintaining commercial, ip and security concerns? What potential impact could they have on discovery productivity? What are the best sustainable business models that can be applied to such services? How significant are the benefits of increased upstream and downstream knowledge flow due to services based on ontology frameworks? What are the key current hindrances to be overcome for the integration of web services into drug discovery in the chemical information area?


Applications of Web-based Services in Drug Discovery

US session chaired by Marc Nicklaus, (National Institutes of Health)
eCheminfo InterAction Meeting Session, Philadelphia, 11 October 2005

Presenters & Discussion Leaders:
Brett Tounge (Johnson & Johnson)
Brad Feuston (Merck)
Marc Nicklaus (National Institutes of Health)
John Irwin (UCSF)
Steve Bryant (NCBI)
David Covell (NCI)

European session chaired by Kim Henrick (European Bioinformatics Institute)
eCheminfo InterAction Meeting Session, Basel, 10 November 2005

Presenters & Discussion Leaders:
Dimitris Dimitropoulos, European Bioinformatics Institute
Johann Gasteiger, Universitaet Erlangen-Nuernberg
Simon Coles, University of Southampton
Eugene Krissinel, European Bioinformatics Institute
Torsten Schwede, University of Basel

Come join us in Philadelphia or Basel for what promises to be intriguing scientific discussions on the ways forward in Web services leading to actions for the benefit of drug discovery researchers!

Barry Hardy
eCheminfo Community of Practice Manager

Communities of Practice

eCheminfo Chairs, Presenters & Instructors