The Protein and Peptide Science Group

The Protein and Peptide Science Group has set up an email discussion group. Click on the link to sign up for discussions and queries on topics related to protein and peptide science.

Prizewinners for the Young Investigators Awards

Forthcoming Events

Committee Members

Past Meetings

Links

The Protein and Peptide Science Group The Group is both a special interest group of the Biochemical Society and a subject group of the Perkin division of the Royal Society of Chemistry. With a historic basis in peptide chemistry, the interests of the Group has enlarged in recent years to cover protein structure determination, structure prediction, molecular modelling and dynamics, protein separation and characterisation, protein biosynthesis, protein expression, combinatorial synthesis, protein design and engineering, drug-protein interactions and protein structure-function. The Group is also committed to paving the way forward into functional genomics and bioinformatics. The Group's mission is to maintain the logical progression of molecular science through chemistry into biochemistry, biology and medicine. Thus, it has an interdisciplinary approach, representing the protein science interests of chemists, molecular biologists, structural biologists, peptide chemists and biologists and members of the biotechnology, food and pharmaceutical industries.

Forthcoming Events:

Harden Conference

September 10th-12th 2003

St John's College, Oxford

Past Meetings:

Protein-Protein Interactions in London

This meeting was organised jointly by Simon Edwards of the Chemical Biology Forum and Brian Austen of the PPSG group at the convenient location of the Scientific Society Lecture Theatre in Saville Row, London, on Tuesday May 7th, 2002. It was attended by about 70 registrants from industry and academia, with representatives from funding bodies.

Sequencing genomes of a number of species, has identified many thousands of open reading frames, which represent many millions of potential protein-protein contacts. It is now a priority in research to establish the identity of the actual functional protein-protein interactions that take place in cells. Protein interactions involved in disease processes may potentially be targeted by pharmaceutical chemists to develop novel drugs.

The meeting covered a variety of approaches for identifying functional interactions between proteins. Sarah Teichmann (LMB-MRC Cambridge) described how bioinformatics is used to identify partners of multi-domain proteins, stable protein complexes or transiently interacting components. Classification of interacting domains among families and superfamilies of proteins provide useful ways of predicting interactions. Biosensors which detect protein-protein-interactions by surface plasmon resonance or evanescent wave-resonance have been used to purify protein complexes containing the adenomatous polyposis coli tumor suppressor protein (Bruce Catimel, Ludwig Institute, Melbourne, Australia) by virtue of specific interactions with an immobilised peptide. A firm basis for establishing the kinetics of interactions of proteins at biosensor surfaces was described by Robin Leatherborrow (Imperial College, London). Migyue He (Discerna Ltd, Babraham, Cambridge) described methods of preparing protein arrays directly on DNA array chips, using in vitro transcription-translation. By removing termination codons, the polypeptides are conveniently analysed still attached to ribosomes. Steve Cleverley (Ciphergen, Camberley, Surrey) described surface-enhanced protein arrays consisting of chemically and biologically-active surfaces on Maldi plates; applications include capture and mass spectrometry identification of crk SH2-binding domain proteins from whole cell lysates.

The meeting finished with a detailed analysis of interactions functioning among the protein components in the Raf-MEK-ERK pathway, using classical techniques of immunoprecipitation and kinase activity (Walter Kolch, Glasgow). The concluding discussion expressed the need for increased collaborations in chemical biology to develop methods for establishing topography of protein complexes in whole cells, and achieving automation in the preparation and use of protein-array chips

Heriot Watt Meeting

Amyloidogenic Proteins involved in neurodegeneration, and therapeutic implications

8-9 April 2002

Speakers and Organisers at the Colloquium on "Amyloidogenic Proteins and their roles in Neurodegenerative Disease" at Heriot-Watt.



L. Serpell, B. Austen, B. Irvine, B. Caughey, D. Beher, E. Zerovnik, S. Cleverley, L. Masino, A. Doig, T. Wisniewski.

Membrane Active Peptides

Colloquium organised at the University of Bristol in April 2001

Organisers: Brian Austen (London), Parvez Haris (De Montfort)

Protein Aggregation in Birmingham

Parvez Haris and Brian Austen, from the Protein and Peptide special interest group organised a symposium on Protein Folding and Aggregation at the RSC annual convention held at the ICC,Birmingham at the beginning of August.

As the formation of insoluble aggregates is a Phenomenon associated with, and perhaps causing, a number of human diseases, there is a need to understand, control and eliminate the pathways leading to aggregation both to alleviate these diseases and to obtain improved yields of useful correctly-folded recombinant proteins. Intermediates in folding may convert to correctly folded forms, or into protein aggregates (Radford, Leeds).

Stephen Davies (UCL) brought us up to date on the aggregation of polyglutamine repeat sequences expressed in the N-terminal region of the protein Huntingtin in patients with Huntington's Disease, his electron micrographs showed clearly the formation of cytoplasmic and intranuclear inclusions in neuronal cells in Huntington's patients and transgenic animal models. A number of other proteins, such as transcription factors, become trapped in these inclusions, but the mechanisms that damage the neurons, and lead to non-apoptotic cell death remain to be fully elucidated.

Human genetics suggest that aggregation of alpha- synuclein may be a cause of the neurodegeneration seen in Parkinson's Disease, Toxic oligomers and fibrils, seen by em, are produced from alpha-synuclein, its mutant forms and from shorter fragments released from alpha-synuclein by proteolysis (El-Agnaf, Lancaster), The region of alpha-synuclein important for aggregation and toxicity has been tracked down to residues 68-78 (Irvine, Belfast).

Soluble oligomers of cyclic peptides ABri and ADan, released by proteolysis of mutant forms of the BRI-proteins in familial dementias are shown to be apoptotic to neuronal cells in culture, and are prime examples of the amyloid hypothesis normally attached to Alzheimer's Disease (Austen, London). Human cystatin B is an intracellular protease inhibitor that is prone to form fibrils connected to signs of epilepsy. (Zerovnic, Slovenia).

There is a pressing need for techniques capable of detecting oligomerisation and fibril formation, atomic force spectroscopy reveals interesting annular-shaped aggregates formed from alpha-synucleins at impressive resolution (Ding, Harvard), and FT-IR holds great promise for the detection of secondary structure in partially-soluble aggregated proteins (Haris, Leicester).

The high resolving power of Fourier-transform ion cyclotron resonance mass spectrometry shows great promise for studying calcium-bonding proteins (Hoxha, Warwick), whereas there are difficulties in detecting poly-Gln interactions by NMR (Pastore, NIMR). Optimised conditions for folding proteins expressed initially as inclusion bodies in E.coli were formulated by Lilie (Halle), and the conditions required for solving the complex problem of providing a lipid-rich environment for optimal folding of membrane proteins was rationalised by Paula Booth (Bristol).

The prion protein, still continues to fascinate audiences, its copper-binding properties are now firmly established (Brown, Cambridge), whereas the mysterious way in which it contorts itself into an infective and potentially fatal, conformation, is still under computation (Warwicker, UMIST). Post-translational modifications undergone by crystallins, are known to result in aggregation of lens proteins, and the formation of cataracts (Harding, Oxford).

Altogether, this was an exciting meeting in which ideas flowed freely, The group welcome the resurgence of interest in biology, and proteomics, by the RSC in evidence throughout this conference at the ICC.

Transcripts from the symposium should appear in the journal Spectroscopy later this year.

7th International Symposium & Exhibition Solid phase synthesis & Combinatorial Chemical Libraries

Peptides, Glycopeptides, Oligonucleotides, DNA, RNA, PNA, Proteins, etc.
Small Molecule Organic Chemical Diversity, Drug Design, etc
Under the Auspices of Mayflower Trust and the European Peptide Society.

Session 1 Alternative Methods Enabling Native Chemical Ligation Assembly of Proteins Dr Derek Hudson (Biosearch Technologies Inc, Novato, CA, USA) Non-peptide Mimics of Helical Structures: Synthesis of Artificial Peptides and Proteins M. Amblard, N. Raynald, D. Maux, G. Berg�, M. Calmes and Prof Jean Martinez (LAPP, Facult� de Pharmacie, Montpellier, France) Synthesis of Peptide and Reporter Conjugates of Oligonucleotide Analogues Dr Mike Gait (MRC Laboratory of Molecular Biology, Cambridge, England, UK)

Session 2A: Solid Phase Synthesis Supports: Handling, Design, Linkers and Spacers Revolutionising Resin Handling for Solid Phase Synthesis Prof Mark Bradley (University of Southampton, Southampton, England, UK) Synthesis and Application of a Novel Perfluoroalkylsulfonyl (PFS) Linker for the Traceless Synthesis of Aromatics Dr Chris Holmes (Affymax Research, Palo Alto, CA, USA) Recent Advances in Synthesis and Use of High Load Spacer-modified Supports in SPS Dr Wolfgang Rapp (Rapp Polymere GmbH, Tuebingen, Germany)

Session 2B: Solid Phase Peptide and Protein Synthesis (I) Solid Phase Synthesis of Cyclic Peptides from Marine Source: Kahalahide F and Trunkamide A Prof Fernando Albericio (University of Barcelona, Spain) Solid Phase Synthesis, Purification and Characterization of Some Biologically Active Peptides and their Fragments Containing Difficult Sequences Prof Lajos Bal�spiri (Inst. of Chemistry, Hungarian Academy of Sciences, Budapest) Extending Synthetic Access to Proteins with a Complementary Peptide bond Ligation Dr John L. Offer and Philip E. Dawson (The Scripps Research Institute and The Skaggs Institute for Chemical Biology, La Jolla, CA, USA)

Session 3A: New Polymer Development and Combinatorial Strategies Combinatorial Approach to the Design of New Grafted Polymeric Surfaces Dr Nick Ede (Mimotopes Pty, Ltd., Clayton, Vic, Australia) Combinatorial Strategies for Biomedical Polymer Development Dr Steve Brocchini (The School of Pharmacy, University of London, England, UK) Preparation of New Multi-Modal Ion Exchange Media -A Combinatorial Approach Dr Nicolas Thevenin and Jean-Luc Maloisel (Amersham Pharmacia Biotech, Uppsala, Sweden) Combinatorial Chemistry is Scintillating Dr Andrew J Sutherland (Aston University, Birmingham, England, UK)

Session 3B: Solid Phase Peptide and Protein Synthesis (II) Improved Synthesis, Biological Evaluation and Conformational Analysis of New h/r CRH Peptide Analogues Prof Paul Cordopatis (Department of Pharmacy, University of Patras, Greece) Solid Phase Incorporation of Lipidic Side-chains on Peptides Dr Jean-Alain Fehrentz (LAPP, Facult� de Pharmacie, Montpellier, France) Amino Acid and Peptide Diols and their Application in Ligation Robert J Broadbridge and Dr Ram P Sharma (University of Southampton, England, UK) Chemical Ligation of Multiple Peptide Fragments Using Thiazolidine-4-Carboxylic Acid as Cysteine Precursor Dr Matteo Villain*, Jean Vizzavona� and Hubert Gaertner* (* GeneProt Inc., Swiss Branch, Meyrin, Switzerland; � University of Geneva, Switzerland)

Session 3C: Oligonucleotide Synthesis and Modifications Linker Phosphoramidites for the Synthesis of Oligonucleotides on Underivatized Supports either Singly or in Tandem Dr Richard T. Pon, Shuyuan Yu, and Fady Girgis (University of Calgary, Calgary, AB, Canada) Inoffensive Chemistry for Labelling, Immobilisations and Conjugations of Oligonucleotides Dr Duncan Graham (University of Strathclyde, Glasgow, Scotland,UK) Amide Group Assisted 3'-Dephosphorylation of Oligonucleotides Synthesized on Universal A Supports Prof Alex Azhayev (University of Kuopio, Finland) Doubly Labeled Oligonucleotides Through Aqeous Diels-Alder Reactions Dr Andreas Wolter (Proligo Biochemie GmbH, Hamburg, Germany)

Session 4 - (Plenary): Combinatorial Chemistry, Spacial Diversity, Combinatorial Scaffolds Two Decades in Combinatorial Chemistry Prof Dr Arpad Furka (Eotvos Lorand University, Budapest, Hungary) Chemical Libraries with Spacial Diversity and Their Use for the Discovery of Peptido- and Proteinomimetics Prof Chaim Gilon (Hebrew University of Jerusalem, Israel Rapid Generation of Heterocyclic Scaffolds on Solid Support: The Concept, Strategy and Practice Dr Hossain Saneii (Advanced SymTech Inc., Louisville, KY, USA)

Session 5A: Instrumentation for Combinatorial Synthesis Construction of a Flexible and Highly Efficient System for Compound Library Production: Consisting of Robotic Arm with Modular Reactors and Work-up Stations Prof Kiyoshi Nokihara (Shimadzu Scientific Research, Tokyo, Japan) Workbench Automation in Synthesis: From Preparation to a Final Substance Werner Zinsser (Zinsser Analytic GmbH, Rodelheim, Germany) Multistep Parallel Solution-phase Synthesis of Urea and Amide Libraries on the TridentTM System Dr Francesco Spadola, Juergen Swienty-Busch, Sukanta Bhattacharyya and Jeff Labadie (Argonaut Technologies AG, CH-4132 Muttenz-Swizerland)

Session 5B: Genetic Analysis/ High Throughput Synthesis (I) Duplex Scorpion Primers in SNP Analysis and FRET Applications" A. Solinas�, L.J. Brown�, C. McKeen�, J.M. Mellor�, J. Nicol�, N. Thelwell� and Prof Tom Brown (�University of Southampton, England, UK; �Oswel Research Products Ltd, Southampton, England, UK) Matrix-induced DNA Fragmentation for High Throughput MALDI-TOF Analysis of Genomic Sequence Polymorphisms Dr Mikhail S. Shchepinov, M.F. Denissenko, K.J. Smylie, R.J. W�rl, A. L. Leppin, C.R. Cantor and C.P. Rodi (Sequenom, Inc., San Diego, CA, USA) Randomly Assembled Arrays, SNP Analysis, and High Throughput Oligonucleotide Synthesis Dr Michal Lebl (Illumina, Inc, and Spyder Instruments, Inc., San Diego, CA, USA)

Session 5C: Analytical Methods for Combinatorial Libraries Applications of a New Mass Spectrometry Tagging Strategy to Focussed Peptide Libraries Dr Corinne Kay (GlaxoSmithKline, Chemical and Analytical Technologies, Stevenage, England, UK) Using Mass Spectrometry for Identifying Novel Substrates for Proteases Dr Stephen C McKeown (GlaxoSmith Kline, Chemical and Analytical Technologies, Stevenage, England, UK) Towards Analysis of Diverse Post-translational Modification of Proteins Using High Performance Mass Spectrometry Prof Yasatsugu Shimonishi (Protein Research Foundation, Osaka University, Japan) High Resolution Biopolymer Mass Spectrometry: New Perspectives for Analysis of Complex Biological mixtures and Combinatorial Libraries Prof Dr Michael Przybylski (University of Konstanz, Germany)

Session 6A: Solid Phase Synthesis and Application of Peptides for Biosensor Systems Solid Phase Synthesis of Regioselectively-labelled Peptides for Biorecognition Analyses via Biosensors Dr John D. Wade (Howard Florey Institute, University of Melbourne, Vic, Australia) Biosensors and Proteomics: the Role of Large Chemically Synthesized Peptides as Sensor Surfaces Prof Ed Nice (Ludwig Institute of Cancer Research, Melbourne, Vic, Australia)

Session 6B: High Throughput Synthesis (II) High Throughput Antisense - From 96-Well Plate Synthesis of Modified Antisense Oligonucleotides to Cell-based Screening Dr Fran�ois Natt (Novartis Pharma AG, Basel, Switzerland) High Throughput Thematic Library Development and Production Dr Christopher B Cooper (Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, USA)

Session 7A: Biomedically-significant Peptides/ Peptide Interactions Combinatorial Search of High Structural Propensity Oligopeptides Dr Saul Gdanski Jacchieri (A.C. Camargo Cancer Hospital, Sao Paulo, Brazil) Chemical Modification of 'Dimerization Inhibitors' of HIV-1 Protease S. K�nig, Prof Dr H.J. Schramm, W. Schramm, T. Wenger, Ren� Loic�* and B. Badet� (Kliniken Innenstadt, Universit�t M�nchen, and MPI Biochemie, Martinsried, Germany; �ICSN-CNRS, Gif-sur-Yvette, France; [*deceased] ) A Peptide that Binds and Stabilises p53 Core Domain Dr Assaf Friedler, Lars O. Hansson, Dmitry B. Veprintsev, Stefan M.V. Freund and Alan R. Fersht (Cambridge University Chemical Laboratory and Cambridge Centre for Protein Engineering, MRC Centre, Cambridge, UK) The Structure and Neurotoxicity of the Abri Peptide an Amyloid Involved in Familial British Dementia Prof Brian M Austen, Omar El-Agnaf, Joseph Sheridan, Christina Sidera, Giuliano Siligardi�, Rohanna Hussain�, Parvez L Haris�, Sidhara Nagala, Maria Lee (St George's Hospital Medical School, London, England, UK; �King's College, London, England, UK; �De Montfort University, Leicester, England, UK)

Session 7B: Microwave-assisted Synthesis/ Novel Intermediates and Reagents A One-pot Three-step Solution Phase Syntheses of Thiohydantoins using Microwave Heating Liselotte �hberg* and Dr Jacob Westman� (*SIK AB, Uppsala Science Park, Uppsala, Sweden; �Personal Chemistry AB, Uppsala, Sweden) Alpha Amino Aldehydes: Protection as N,O-Acetals for Use as Novel Building Blocks in the Solid Phase Synthesis of Heterocyclic Compounds" Dr J. Beyer and Prof M. Meldal (Carlsberg Laboratory, Valby, Denmark ) Novel Polymer-supported Reagents for Organic Transformations in Solution and for Postmodification of Compound Collections Obtained by Solid Phase Synthesis Dr J�rg Rademan and Prof Dr Guenther Jung (Institute of Organic Chemistry, University of Tuebingen, Germany) EVOblueTM30 as New Red Excitable High Performance Fluorescence Dye for Assay Development and HTS Applications" Dr Eloisa Lopez-Calle, Joachim R. Fries, Annett M�ller and Dirk Winkler (Evotec OAI , Hamburg, Germany) Solid Phase Synthesis of Heterocyclic Ketene Aminals (I) Prof Mei-Xiang Wang, Tao Peng, Chan-Ping Du and Zhi-Tang Huang (Institute of Chemistry, Chinese Academy of Sciences, Beijing , China) Solid Phase Synthesis of Heterocyclic Ketene Aminals (II) Prof Zhi-Tang Huang, Zhen-Dong Liu, Li-Ping Xing and Mei-Xiang Wang (Institute of Chemistry, Chinese Academy of Sciences, Beijing , China)

Prizewinners for the Young Investigators Awards

Biochemical Society/Portland Press Third Floor Eagle House 16 Procter Street London WC1V 6NX United Kingdom Map Biochemical Society Registered Company Number 892796 limited by guarantee VAT No. GB 523 2392 69 Registered Charity Number 253894 Portland Press Ltd Registered Company Number 2453983 Vat No GB 523 2392 69 Biochemical Society Membership Office Portland Customer Services Commerce Way Whitehall Industrial Estate Colchester Essex CO2 8HP United Kingdom Map

Administration: Tel: 020 7280-4100 - Fax: 020 7280-4170 E-mail: [email protected] Editorial: Tel: 020 7280-4110 - Fax: 020 7280-4169 E-mail: [email protected] Meetings: Tel: 020 7280-4150 - Fax: 020 7280-4167 E-mail: [email protected] Membership: Tel: 01206 796 351 - Fax: 01206 799 331 E-mail: [email protected] Customer services: Tel: 01206 796 351 - Fax: 01206 799 331 E-mail: [email protected] Read our Privacy Policy