Scientific Program

Keynote and Plenary Speakers

Session I: Peptide and Protein Synthesis Strategies

NEW APPROACHES FOR SEQUENCE SCANNING TO IDENTIFY SECONDARY STRUCTURE IMPORTANT FOR PEPTIDE BIOLOGY
Professor William D. Lubell obtained his B.A. degree in Chemistry from Columbia College and his Ph.D. in 1989 from the University of California in Berkeley under the supervision of Professor Henry Rapoport. A fellow of the Japan Society for the Promotion of Science, he studied with Professor Ryoji Noyori at Nagoya University in Nagoya, Japan. In September of 1991, he joined the faculty at l'Université de Montréal in Québec, Canada where he is now Full Professor. His research interests focus on the development of solution and solid-phase methods for synthesizing enantiopure heterocycles, amino acids and peptide mimics, and their application in catalysis, chemical biology and medicinal chemistry.

PEPTIDE-BASED CATALYSTS FOR ASYMMETRIC REACTIONS
Scott J. Miller was born December 11, 1966 in Buffalo, NY. He received his B.A. (1989), M.A. (1989) and Ph.D. (1994) from Harvard University, where he worked in the laboratories of Professor David Evans as a National Science Foundation Predoctoral Fellow. Subsequently, he traveled to the California Institute of Technology where he was a National Science Foundation Postdoctoral Fellow in the laboratories of Professor Robert Grubbs. In 1996, he joined the faculty at Boston College, where he is now Professor of Chemistry. His awards and honors include: National Science Foundation CAREER Award (1999); Cottrell Scholar Award (1999) and Research Innovation Award (1998) of Research Corporation; Alfred P. Sloan Research Fellowship (2000); Camille Dreyfus Teacher-Scholar Award (2000); DuPont Young Professor Award (2000); Novartis Chemistry Lectureship Award (2000); GlaxoSmithKline Chemistry Scholar Award (2000); Lilly Grantee Award (2000); Merck Chemistry Council Support (2001); Pfizer Award for Creativity in Organic Chemistry (2003); Arthur C. Cope Scholar Award of the American Chemical Society (2004).

CONSTRUCTION OF COMPLEX PROTEINS AND GLYCOPROTEINS USING CHEMICAL LIGATION
Phil Dawson is an Assistant Professor in the departments of Cell Biology and Chemistry at The Scripps Research Insititute, La Jolla, CA. He received his B.A. in Chemistry from Washington University, St. Louis, MO in 1992 and did his doctoral work with Stephen B.H. Kent at the Scripps Research Insitute, graduating in 1996. Following postdoctoral work at Caltech with Harry B. Gray, he returned to Scripps in 1997 as a member of the Skaggs Institute for Chemical Biology. He received an Alfred P. Sloan award (2001) and is on the Editorial Boards of Peptide Letters and The International Journal of Peptide Research and Therapeutics. He is the Chairman of the Travel Award Committee for this Symposium. Dr. Dawson is a member of the American Chemical Society, American Association for the Advancement of Science, FASEB: Protein Society, and the American Peptide Society. He has published over 50 manuscripts and 2 patents. Dr. Dawson's research focuses on using synthetic protein chemistry to address fundamental questions in the areas of protein folding, stability and enzymatic catalysis. Other research interests include HIV vaccine design and protein post translational modifications. In addition, his laboratory has continued to develop synthetic methodology with the goal of improving the accessibility of proteins to synthetic chemistry.

Session II: Biosynthesis of Bioactive Peptides

REASSIGNING SENSE CODONS FOR RIBOSOMAL SYNTHESIS OF NOVEL TEMPLATE ENCODED POLYMERS
Stephen Blacklow entered the M.D., Ph.D. program at Harvard Medical School and carried out thesis research in the Department of Chemistry in the laboratory of Dr. Jeremy Knowles. After receiving his degrees in 1991, he entered a Pathology residency at the Brigham and Women's Hospital, and joined the laboratory of Peter Kim in 1993 (at the Whitehead Institute) for his postdoctoral studies. He is currently an Associate Professor of Pathology at Brigham and Women's Hospital and Harvard Medical School, where his research program focuses on receptor biochemistry and on mechanistic aspects of translation.

PEPTIDE MODULATORS OF G PROTEIN SIGNALING
Richard W. Roberts earned a B.S. in chemistry from the University of Kansas in 1987 and a Ph.D. in Chemistry from Yale University, under Donald M. Crothers, in 1993. He then pursued postdoctoral work at Harvard Medical School/MGH with Prof. Jack W. Szostak as an Alfred P. Sloan Foundation and NIH postdoctoral fellow. In 1997 he joined the chemistry faculty at Caltech where his laboratory uses mRNA display, a selection technique he invented, for the purpose of peptide, protein, and peptide-mimetic design. His awards include a Beckman Young Investigator Award, an NSF PECASE award, and Alfred P. Sloan Foundation Fellowship.

CHEMOENZYMATIC APPROACHES TO NEW PEPTIDE ANTIBIOTICS
Mohamed A. Marahiel studied chemistry at the Universities of Cairo (Egypt) and Goettingen (Germany). In 1977, he obtained a PhD in biochemistry and microbiology from the University of Goettingen, where he carried out his research work at the Max Planck Institute for Experimental Medicine. Subsequently, he received an assistant professor's position at the Technical University of Berlin, where in 1987 he obtained his Habilitation in biochemistry at the Institute of biochemistry and molecular biology. Three years later he moved to the Philips-Universitaet Marburg as a professor of biochemistry in the chemistry department. He was a Deutsche Forschungsgemeinschaft fellow in 1978 and 1986 at the John Innes Institute in Norwich (UK) and at the Bioloabs, Harvard University (USA), respectively. His present research focuses on the structure-function relationship and on the elucidation of reaction mechanisms of modular peptide synthetases involved in the nonribosomal synthesis of peptide antibiotics, as well as on the rational design of recombinant enzymes for the synthesis of novel bioactive peptides. His group is also interested in studying the function and regulation of the major cold shock proteins in soil bacteria as well as other stress-induced proteins.

SYNTHESIS AND BIOLOGICAL ASSESSMENT OF INSULIN-LIKE ANALOGS WITH DIFFERENTIAL ACTIVITY AT THE INSULIN AND IGF-1 RECEPTORS
Richard DiMarchi is the Linda & Jack Gill Chair in Biomolecular Sciences and Professor of Chemistry at Indiana University. He is a retired Group Vice President at Eli Lilly & Company where for more than two decades he provided leadership in biotechnology, endocrine research and product development. He currently serves as a co-founder and Board Chairman of Ambrx, Inc. He previously served as a board member to the biotechnology trade group BIO and the American Peptide Society, as well as such companies as Millennium Biotherapeutics and Inproteo. He currently serves as Board member to Isis Pharamceuticals, and scientific advisor to Alba Inc., Semafore Pharmaceuticals and Epitome Biosciences. Professor DiMarchi is readily recognized for discovery and development of rDNA-derived Humalog® (LisPro-human insulin). This designer insulin represents the first demonstration that structurally altered rDNA-derived biosynthetic proteins can improve pharmacological performance without increasing the risk of an abnormal immunological response. As scientist and administrator Dr. DiMarchi was a leading force in the discovery and commercial development of Xigris®, and Forteo®. The goal of his current research and commercial endeavors is to develop proteins with enhanced therapeutic properties through biochemical optimization with non-natural amino acids, an approach he has termed chemical-biotechnology.

Opening Keynote: AN EXPANDED GENETIC CODE

Peter G. Schultz graduated (summa cum laude) from Caltech in 1979 and continued there for his doctoral degree (in 1984) with Professor Peter Dervan. He then spent a year at the Massachusetts Institute of Technology with Professor Christopher Walsh before moving to the University of California, Berkeley, and the Howard Hughes Medical Institute. He is currently the Scripps Professor of Chemistry at The Scripps Research Institute and Director of the Genomics Institute of the Novartis Research Foundation. Schultz has made a number of major contributions to science including: (1) the discovery of catalytic antibodies, and their use to study fundamental mechanisms of biological catalysis and the evolution of binding and catalytic function; (2) the development of technology that for the first time enables the systematic expansion of the genetic codes of living organisms to include unnatural amino acids beyond the common twenty; and (3) the development and application of combinatorial methods in chemistry and biology including the first generation of combinatorial materials libraries and the isolation of molecules that control stem cell proliferation and fate. Schultz has received numerous awards including the Alan T. Waterman Award, NSF (1988), the ACS Award in Pure Chemistry (1990), the Wolf Prize in Chemistry (1994), and the Paul Erhlich and Ludwig Darmstaedter Award (2002). Professor Schultz is a member of the National Academy of Sciences, USA (1993) and the Institute of Medicine of the National Academy of Sciences (1998). He is active on many editorial and scientific advisory boards and is a founder of Symyx Technologies, Affymax, Syrrx, Kalypsys, Phenomix, Ambrx and Ilypsa.

Session III: New Themes in Antimicrobials and Quorum Sensing

THREADED RINGS AND COMPLEX TOPOLOGIES IN NOVEL ANTIMICROBIAL PEPTIDES: NATURE'S BIO-ENGINEERING TEMPLATES
David Craik is an Australian Research Council Professorial Fellow at the Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia. He is the author of more than 270 refereed publications and is lead inventor on three patents. He is a member of the editorial boards of Current Medicinal Chemistry, the Encyclopedia of Spectroscopy and Spectrometry, The Handbook of Modern Magnetic Resonance, Peptide and Protein Letters, and Bioplymers: Peptide Science. He is editor of the book NMR in Drug Design. His contributions to medicinal chemistry and NMR have been recognised by the award of the Adrien Albert medal of the Royal Australian Chemical Institute and the ANZMAG medal of the Australian and New Zealand Society of Magnetic Resonance. His research interests focus on the application of NMR in drug design, and on toxins, including conotoxins. His group has a particular focus on structural studies of disulfide-rich proteins, and on the discovery and applications of circular proteins and novel protein topologies. He is founder of Kalthera Pty Ltd and Cyclagen Pty Ltd, Brisbane-based biotechnology companies that are developing pharmaceutical and agricultural applications, respectively, of a family of circular proteins called the cyclotides.

A MINIMALIST APPROACH TO ANTIMICROBIAL AGENTS WITH THIONIN AS A TEMPLATE
David Andreu studied chemistry at the University of Barcelona, where he got a Ph.D. in organic chemistry in 1981 (with E. Giralt). He was research associate with Bruce Merrifield at Rockefeller University from 1982 to 1985. In late 1985 he rejoined the University of Barcelona as associate professor of Organic Chemistry and continued in that capacity until 2001, when he accepted a position as professor of chemistry and head of the proteomics facility at the Pompeu Fabra University, also in Barcelona. David's interests along those years have focused largely on synthetic peptides and their biomedical applications, particularly as vaccines and antibiotics. These remain active research topics in his current laboratory, where new research lines on proteomics are also being pursued. David is coauthor of over 160 papers and reviews on bioactive peptides and related areas. He serves on the Executive Committee of the European Peptide Symposium, as Scientific Affairs Officer.

ANTIVIRAL CYCLIC DL-a-PEPTIDES: TARGETING A GENERAL BIOCHEMICAL PATHWAY IN VIRUS INFECTIONS
Reza Ghadiri is Professor, Departments of Chemistry and Molecular Biology, and Member of the Skaggs Institute for Chemical Biology, at The Scripps Research Institute. He received his B.A. in Chemistry from University of Wisconsin-Milwaukee in 1982 and Ph.D. in 1987 in Synthetic Organic Chemistry with Professor B. M. Trost at the University of Wisconsin-Madison. Dr. Ghadiri joined the faculty of The Scripps Research Institute in 1989 after completing a postdoctoral appointment at the Rockefeller University in the laboratory of Professor E. T. Kaiser. Dr. Ghadiri's research interests include: de novo design of synthetic proteins and enzymes; self-assembling peptide nanotubes and biomaterials; synthetic transmembrane ion channels and antimicrobial agents; novel biosensors; self-replicating molecular systems and self-organized chemical networks; and molecular computation. He is a recipient of the Searle Scholars Award, Arnold and Mabel Beckman Young Investigator Award, Alfred P. Sloan Research Fellowship, American Chemical Society Award in Pure Chemistry, Feynman Prize in Nanotechnology, Arthur C. Cope Scholar Award, and Elected Fellow of the American Association for the Advancement of Science. He serves on the editorial advisory board of three scientific journals and is an active consultant for pharmaceutical and biotech companies.

QUORUM SENSING AND INTERFERENCE BY BACTERIAL AUTOINDUCING PEPTIDES
Richard Novick received his MD from NYU, with honors in microbiology, and spent 2 post-doctoral years with the late Martin Pollock at the NIMR in London, where he discovered antibiotic resistance plasmids in S. aureus. This led to a long-term interest in plasmids, in antibiotic resistance, and in the pathobiology of the staphylococci. He is widely regarded as a founding father of the field of plasmid biology and is the founding editor of the journal PLASMID. He also contributed seminally to the development of the molecular biology of the staphylococci, editing a book by that name in 1990. His most recent focus has been on the regulation of staphylococcal pathogenesis, exemplified by his discovery of a major regulatory system, the agr system, that governs the expression of most of the staphylococcal virulence genes. This system is autoinduced by a unique thiolactone peptide, which has been the object of a very productive collaboration with Tom Muir, and which is the subject of his talk. Dr. Novick is currently Professor of Microbiology and Medicine at the Skirball Institute of the NYU Medical Center, and is an Adjunct Professor at Rockefeller University.

POST-TRANSLATIONAL MODIFICATIONS DURING LANTIBIOTIC BIOSYNTHESIS
Wilfred van der Donk received his B.S. and M.S. from Leiden University, The Netherlands under the guidance of Prof. Jan Reedijk and his Ph.D. from Rice University in the laboratories of Prof. Kevin Burgess. After postdoctoral work with Prof. JoAnne Stubbe at MIT, he joined the faculty at the University of Illinois at Urbana-Champaign in 1997. The research in his laboratory focuses on understanding of the molecular mechanisms of enzyme catalysis and the use of enzymes for antibiotic synthesis.

Merrifield Award and Lecture : FROM TENS TO TRILLIONS : ADVANCES IN SYNTHETIC COMBINATORIAL AND DIVERSITY ORIENTED METHODS OVER THE PAST 20 YEARS

Richard A. Houghten received his doctorate in organic chemistry from the University of California, Berkeley, in 1975. Following positions at the University of California, San Francisco, and Mount Sinai School of Medicine, he joined the Scripps Research Institute in 1981. In addition to Torrey Pines Institute for Molecular Studies, he founded three commercial businesses, one of which became a publicly-traded biotechnology company. His achievements have been recognized in the form of numerous honors and awards. Most recently, his contribution to the field of peptide science was acknowledged by the 2004 Ralph F. Hirschmann Award in Peptide Chemistry. Other honors received include the Vincent du Vigneaud Award for Excellence in Peptide Science (2000) and the UCSD Connect Athena Pinnacle Award for Empowering Women in the Workplace. Dr. Houghten's scholarly contributions include over 500 publications and 60 issued patents. He also founded the journal, The Journal of Peptide Research and is active on several other editorial boards. Dr. Houghten's scientific contributions include the "tea bag" approach, which was originally utilized to facilitate the synthesis of peptides. In collaboration with his long time associates and colleagues at Torrey Pines Institute for Molecular Studies, he has also developed approaches in combinatorial chemistry which are invaluable for the rapid identification of individual compounds from millions to billions of others (positional scanning), the use of existing combinatorial libraries to generate entirely new diversities of compounds (libraries from libraries), the cross-referencing of library screening results with gene data bases in order to fine-tune the direction towards which further testing moves for a given disease target (biometrical analysis), and novel volatilizable solid supports.

Session IV: Post-Translational Modifications of Peptides and Proteins

CHEMICAL APPROACHES TO SORTING OUT PROTEIN PHOSPHORYLATION
Phil Cole graduated from Yale University with a B.S. in Chemistry in 1984. Following a year spent as a Churchill Scholar in Cambridge, he pursued MD-PhD studies at Johns Hopkins, graduating in 1991. His PhD research was carried out in Cecil Robinson's lab in the Dept. of Pharmacology and concerned chemical approaches to aromatase mechanism and inhibition. He then went on to complete residency training in Medicine at Brigham and Women's Hospital in Boston in 1993. From 1993-1996, Cole was a postdoctoral research fellow in Chris Walsh's lab at Harvard and a clinical endocrine fellow at the Brigham. In 1996, Cole moved to Rockefeller University as assistant professor and head of the lab of Bioorganic Chemistry. In 1999, he returned to Hopkins as director of Pharmacology and E.K. Marshall and T.H. Maren professor. His research career has focused on the application of chemical methods to address biomedical problems. His group's scientific achievements include the development, in collaboration with Tom Muir, of a simple and widely used method to carry out protein semi-synthesis called expressed protein ligation. His lab has applied this method to study the detailed aspects of protein phosphorylation and acetylation. In addition, his group has demonstrated that there is a dissociative transition state in protein kinase reactions and has used this model to design the first potent mechanism-based protein kinase inhibitors. Cole's lab also developed the first selective melatonin rhythm enzyme and HAT (histone acetyltransferase) enzyme inhibitors which are currently being employed to study circadian rhythm and gene regulation, respectively. Cole's group has been the first to chemically rescue a mutant enzyme (protein tyrosine kinase) in living cells and is exploiting this strategy in the analysis of cell signal transduction pathways. Among his honors include a Damon-Runyon Scholar Award, a Burroughs-Wellcome Award in Toxicology, and an Ellison Medical Foundation Award.

PROTEIN SEMI-SYNTHESIS AND ITS APPLICATION TO STUDIES OF STRUCTURE AND FUNCTION OF GTPASES
Kirill Alexandrov, born 1967 in Leningrad, USSR. Received MS in Zoology/Parasitology, at the State University of Leningrad in 1989. Received a Ph.D. in Cell Biology at the European Molecular Biology Laboratory, Heidelberg, Germany in 1995. Postdoctoral training 1996- 1999 at the Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology Dortmund, Germany. Since 1999 a group leader in the same department.

CHEMICAL APPROACHES TO STUDYING PROTEIN GLYCOSYLATION IN THE BRAIN
Linda Hsieh-Wilson received her B.S. in chemistry from Yale University in 1990. She received her Ph.D. in chemistry from the University of California at Berkeley where she was a National Science Foundation and American Chemical Society fellow in the laboratory of Professor Peter G. Schultz. In 1996, she moved to Rockefeller University to study neurobiology with Professor Paul Greengard as a Damon Runyon-Walter Winchell postdoctoral fellow. Linda joined the chemistry faculty at the California Institute of Technology in 2000, where her laboratory studies how the molecular structure of carbohydrates encodes functional information in the brain. Her awards include a Beckman Young Investigator Award, an NSF CAREER Award, and an Alfred P. Sloan Foundation fellowship.

Session V: Goodman Memorial Session

MURRAY GOODMAN: PROFESSOR

Joseph P. Taulane received his BA at the University of California , San Diego, and his MSc at UC, Santa Barbara under T.C. Bruice doing flavin redox kinetics. He returned to UCSD in 1977 to work in the laboratories of Murray Goodman. He has remained in the Goodman group to the present in the role of Laboratory Director. In this capacity he assisted Professor Goodman in guiding graduate students and postdoctoral fellows with their research projects in laboratory theme areas such as the opioids and somatostatin. His primary expertise is in the purification and characterization of peptides and related structures. In recent years his research efforts have been focused on studies of collagen-mimetic structures and guanidine-containing transport molecules.

PROFESSOR MURRAY GOODMAN: A PIONEER OF PEPTIDE SCIENCE

Fred Robert Naider: B. Ch. Eng. and M.S. Ch. Eng. from Cornell University, Ph.D. in Polymer Chemistry with Murray Goodman at the Brooklyn Polytechnical Institute, Postdoc at the Weizmann Institute in Biophysics. I began my academic career at the College of Staten Island, CUNY, focusing first on peptide transport and then on signal transduction through G protein-coupled receptors. We synthesize, biosynthesize and study the structure of peptide hormones and receptor fragments using biophysical methods including, CD, IR, NMR and fluorescence spectroscopy. Currently I am Distinguished Professor of Chemistry and Biochemistry at CUNY. I am the APS representative to the Public Affairs Executive Committee of FASEB and I Chair the Breakthroughs in Bioscience subcommittee of the Science Policy Committee of FASEB. I am a permanent member of the SBCB Study Section for NIH. My laboratory collaborates with that of Jeffrey M. Becker, a microbiologist at the University of Tennessee. We have had continuous NIH support for 30 years and contributed about 200 refereed publications to the literature.

PEPTIDES IN THE DAYS OF PHOTONICS

Luis Moroder was born at St. Ulrich in Italy in 1940. He had his early training in peptide chemistry with Professor E Scoffone at Padua and then as postdoc with Professor K Hofmann in Pittsburgh. He joined in 1975 the Department of Peptide Chemistry headed by Professor E. Wünsch at the Max-Planck-Institute of Biochemistry, Martinsried, and since 1991 he has been Head of the Laboratory of Bioorganic Chemistry at this Institute. He has been awarded the Max Bergman Medal, and in 2004 was Josef Rudinger Lecturer of the European Peptide Society. He is author or co-author of over 500 publications in diverse research fields which currently include hormone receptors, collagen peptides, proteinase inhibitors and photomodulation of peptide properties as well as the area of protein engineering with non-natural amino acids. As editor of the five volume Houben-Weyl compendium on Synthesis of Peptides and Peptidomimetics he contributed in assessing the state of the art in the field.

IT ALL STARTED IN BROOKLYN FORTY-FIVE YEARS AGO!

Claudio Toniolo is currently Professor of Organic Chemistry at the Department of Chemistry, University of Padova, Italy. With Murray Goodman he was post-doctoral fellow at the Polytechnic Institute of Brooklyn, NY, in 1967/68, and Visiting Professor at UCSD in 1984. He is author or co-author of more than 660 publications on peptide synthesis and conformation, peptidomimetic foldamers, rigid peptide-based templates and bridges, and membrane-active peptaibol antibiotics. He is the current Italian representative in the EPS, member of the editorial committees of numerous journals on bioorganic chemistry and peptide science, and co-editor (with Murray Goodman et al.) of the recently published Houben-Weyl volume series on peptide and peptidomimetic synthesis.

PEPTIDE APPROACHES TO FOLDING AND ASSEMBLY OF TRANSMEMBRANE HELICES IN PROTEINS

Charles Deber received his BSc at Brooklyn Poly with Murray Goodman, his PhD at MIT under Arthur C. Cope, and was a post-doctoral fellow with Elkan Blout at Harvard Medical School. He is currently Professor of Biochemistry at the University of Toronto, and Senior Scientist in the Division of Structural Biology & Biochemistry in the Research Institute at the Hospital for Sick Children in Toronto. Dr. Deber's career-long research approach has involved the application of peptide chemistry to biochemical phenomena, to deduce experimentally how sequence confers protein structure and function. In recent years, he has applied this approach to study of the amino acid 'motifs' which determine helix-helix interactions between segments in the membrane domains of proteins with the goal of deciphering the molecular basis for misfolding defects that often lead to disease states. Dr. Deber received the Vincent duVigneaud Award of the American Peptide Society in 2000, and the following year, he was elected a Fellow of the Royal Society of Canada, giving him membership in the Canadian Academy of Sciences.

OPIOID PEPTIDE ANALOG DESIGN: FROM CYCLIC ENKEPHALINS TO ORALLY ACTIVE ANALGESICS

Peter Schiller studied chemistry at the Swiss Federal Institute of Technology (ETH) in Zurich, where he obtained his doctorate under the direction of Robert Schwyzer. After postdoctoral training at the Johns Hopkins University (Ludwig Brand) and at NIH (Chris Anfinsen), he assumed his present position at the Clinical Research Institute of Montreal (IRCM) as Director of the Laboratory of Chemical Biology and Peptide Research in 1975. He holds a concurrent position as Professor of Pharmacology at the University of Montreal. During the past 30 years his research has been focused on structure-activity relationships of peptide hormones and neurotransmitters. He has used an interdisciplinary approach, incorporating organic synthesis, peptide chemistry, pharmacological testing and conformational studies, to develop new concepts in peptide drug design. His research efforts in the opioid peptide field resulted in the discovery of highly receptor-specific agonists and antagonists, and of novel mixed agonist/antagonists. Some of these compounds are widely used as pharmacological tools in opioid research or are being pursued as drug candidates. He has authored over 320 publications and 12 patents. He was President of the American Peptide Society (1995-97) and Chair of the Section on Drug Design and Discovery of the American Association of Pharmaceutical Scientists (AAPS) (2003). He co-chaired the Peptide Gordon Conference in 1992 and served on numerous NIH study sections during the past 20 years. He is a Fellow of the Royal Society of Canada (Academy of Science), of the AAAS and of the AAPS. He received several awards, including the Max-Bergmann Medal, the Galen Award (Prix Galien) of Canada, an NIH MERIT Award, the Vincent du Vigneaud Award, and the AAPS Research Achievement Award in Medicinal and Natural Products Chemistry.

MURRAY GOODMAN: FORMIDABLE SENIOR FIGURE, FRIENDLY COLLEGIATE PEER, FATHERLY AND GENEROUS MENTOR

Richard A. Houghten received his doctorate in organic chemistry from the University of California, Berkeley, in 1975. He is the founder and President of Torrey Pines Institute for Molecular Studies. In addition to Torrey Pines Institute for Molecular Studies, he also founded three commercial businesses, one of which became a publicly-traded biotechnology company. Dr. Houghten has authored over 500 scientific publications and is an inventor on more than 60 issued patents. His achievements have been recognized in the form of numerous honors and awards which include the 2005 Merrifield Award, the Ralph F. Hirschmann Award in Peptide Chemistry (2004), and the Vincent du Vigneaud Award for Excellence in Peptide Science (2000).

Session VI: Towards Peptides as Potential Therapeutics I

TARGET-BASED PROTEOLYTIC PROFILING FOR CHARACTERIZING CANCER PROGRESSION.
Gregg B. Fields received a Ph.D. degree in chemistry from Florida State University in 1988. He was a Postdoctoral Scholar with Ken A. Dill at the University of California San Francisco from 1989-1990, and during that time served as a Visiting Scientist at Applied Biosystems. Fields joined the faculty at the University of Minnesota in 1991 as an assistant professor. He was promoted to associate professor with tenure in 1995 and then achieved his present rank of full professor of chemistry & biochemistry at Florida Atlantic University in 1997. Fields assumed the duties of department chair in 2000. His research interests are in the use of chemical approaches to better understand how protein three-dimensional structures influence cellular and enzymatic behaviors. Fields' work has led to the "collagen structural modulation" model for metastatic melanoma cell invasion, in which the progression of melanoma cell events is dictated by the structural state of basement membrane collagen. These studies have provided insights into the mechanisms of melanoma cell behavior as well as identifying metalloproteinases produced by melanoma cells. Mini-protein models have subsequently been utilized to dissect the mechanisms of collagen catabolism, and in the process have provided new avenues for protease inhibitor design. Fields has authored or coauthored more than 170 scientific publications and presented ~100 invited lectures. His honors and awards include a McKnight-Land Grant Professorship (1993), a National Institutes of Health Research Career Development Award (1994), an Association of Biomolecular Resource Facilities Excellence Award in Peptide Synthesis Research (1997), Florida Atlantic University's Researcher of the Year (2000-2001), and appointment as a Distinguished Visiting Professor at Imperial College London (2004).

FROM SIMPLE CONSENSUS PEPTIDES TO HIGH AFFINITY LIGANDS: A STEPWISE DIVERSITY-ORIENTED STRATEGY FOR THE ACQUISITION OF POTENT SIGNALING INHIBITORS.
David S. Lawrence received his B.S. in Biological Sciences at the University of California at Irvine and subsequently earned his Ph.D. from UCLA in natural products synthesis with Robert V. Stevens. He was a postdoctoral fellow in the laboratory of E. Thomas Kaiser at the Rockefeller University. In 1985 he joined the Department of Chemistry at SUNY Buffalo as a faculty member and subsequently, in 1995, moved to the Albert Einstein College of Medicine, where he is currently a Professor of Biochemistry.

Session VII: Peptide and Protein Design

CONFORMATIONAL DIVERSITY AND CATALYSIS
Donald Hilvert: B.A., Brown University, 1978; Swiss Universities Predoctoral Fellow, 1979; Ph.D., Columbia University, 1983; Postdoctoral Fellow, Rockefeller University, 1984-85; Assistant, Associate and Full Professor of Chemistry and Molecular Biology, The Scripps Research Institute, 1986-1997. Since 1998, Professor of Chemistry, Swiss Federal Institute of Technology (ETH), Zurich, Switzerland. Research Interests: Enzyme reaction mechanisms; design and chemical synthesis of proteins; artificial enzymes; directed evolution. Honors: Alfred P. Sloan Research Fellow, 1991-93; American Chemical Society Arthur C. Cope Scholar Award, 1992; Fellow of the American Association for the Advancement of Science, 1993; Pfizer Award in Enzyme Chemistry, 1994; Merck Lecturer, Cambridge University, 2001; Novo Nordisk Lecturer, Danish University of Pharmaceutical Sciences, 2003; Fellow of the Royal Society of Chemistry, 2004; Editor, Current Opinion in Chemical Biology.

FUNCTIONALIZED POLYPEPTIDES FOR PROTEIN RECOGNITION
Lars Baltzer is a Full Professor of Organic Chemistry at Uppsala University since 2004, after having served previously as Full Professor of Organic Chemistry at Linköping University and as Full Professor of Organic Chemistry at Göteborg University. Lars Baltzer is a member of the Council of the European Peptide Society and a member of the Board of the European Society of Combinatorial Science. The research interests of Lars Baltzer are centered around protein design and functionalization with special emphasis on molecular recognition and catalysis.

DESIGNED PEPTIDE MICROARRAYS FOR PROTEIN DETECTION AND CHARACTERIZATION
Hisakazu Mihara, Dr.Sc. He received his Dr.Sc. in Chemistry in 1986 at Kyushu University at Professor Nobuo Izumiya Lab. He was a postdoctoral fellow at Professor Emil T. Kaiser Lab of the Rockefeller University from 1986 - 1988. He was appointed as an Assistant Professor in Applied Chemistry at Kyushu Institute of Technology in 1988, and promoted to an Associate Professor in Applied Chemistry at Nagasaki University in 1993. Currently, he has been involved in Department of Bioengineering, Tokyo Institute of Technology, from 1995. He is a member of Japanese Peptide Society and American Peptide Society.

PROBING MINIPROTEIN STABILITY VIA BACKBONE THIOESTER EXCHANGE
Samuel H. Gellman earned his A.B. from Harvard University in 1981 and his Ph.D. at Columbia University, under Ronald Breslow, in 1986. After an NIH post-doctoral fellowship at the California Institute of Technology, with Peter Dervan, Gellman joined the faculty at the University of Wisconsin - Madison as an Assistant Professor in 1987. He was promoted to Associate Professor in 1993 and to Professor in 1995. Gellman is currently Evan P. Helfaer Professor of Chemistry and serves as Chair of the Organic Division in the Department of Chemistry. Among Gellman's honors is an Arthur C. Cope Scholar Award from the American Chemical Society in 1997. Gellman's service to the chemical community has included a term on the National Institutes of Health Medicinal Chemistry Study Section (1999-2002). He is a member of the editorial advisory boards of the Journal of Organic Chemistry, the European Journal of Organic Chemistry, Biomolecular & Organic Chemistry, Biopolymers-Peptide Science and Chemical Society Reviews.

Session VIII: Peptide Quaternary Structures in Material Science and Disease

DESIGNING NANO-TO-MICRON SCALE PEPTIDE-BASED SELF-ASSEMBLING SYSTEMS FROM THE BOTTOM UP
Dek Woolfson obtained his BA in Chemistry from the University of Oxford, UK (1987), and his PhD in Chemistry from University of Cambridge, UK (1992). Early is his academic career he developed an interest the folding and structures of peptides and proteins. His pre-doctoral work included experimental studies of the kinetics and thermodynamics of the folding of peptide fragments and intact natural proteins. His post-doctoral work included establishing sequence-to-structure relationships for various protein-folding motifs, and testing these experimentally. During this time he became interested protein engineering and design. Over the past ten years he has established an independent research group at the University of Sussex, which is focused on the de novo design of peptides and proteins, and its application in bionanotechnology. Current design targets in the Woolfson laboratory include: self-assembling peptide fibres, tubes and matrices; peptide-based switches and sensors; and protein-based receptors for small-molecule ligands of biomedical interest.

MECHANISMS OF AMYLOIDOGENESIS
Evan Powers received his bachelor's degree in chemistry from Cornell University in 1992. He did his doctoral studies with Daniel Kemp at the Massachusetts Institute of Technology, and received his Ph. D. in 1999. He went on to do post-doctoral research with Jeffery Kelly at The Scripps Research Institute, where he has remained since as an Assistant Professor.

CYTOCOMPATIBILITY AND ANTIMICROBIAL ACTIVITY OF SELF-ASSEMBLED BETA HAIRPIN HYDROGELS
Joel Schneider, associate professor of chemistry and biochemistry, earned his B.Sc. in Chemistry at the University of Akron and a Ph.D. in chemistry at Texas A&M University under the guidance of Jeffery Kelly. After which, he joined William DeGrado at the University of Pennsylvania as a George W. Raiziss Postdoctoral Fellow. He joined the department of Chemistry and Biochemistry at the University of Delaware in 1999 with a secondary appointment in the department of Materials Science and Engineering. He currently serves on the editorial advisory board of Peptide Science. His research entails the design of functional peptides and proteins. Of current interest is the development of environmentally responsive peptide-based hydrogel materials for use in tissue engineering.

Makineni Award and Lecture : MEDICINAL CHEMISTRY APPLIED TO A SYNTHETIC PROTEIN : THE PREVENTION OF INFECTION BY HIV

Robin Offord began in nuclear physics but soon changed to biology. He first worked at the Medical Research Council Laboratory, Cambridge, U.K. (1962-1966), in the group Frederick Sanger where he obtained his Doctorate and collaborated with, among others, César Milstein and Aaron Klug. He taught and researched at Oxford from 1966 - 1980 (University Lecturer in Molecular Biophysics, Tutor, Christ Church), when he left to become Director of the Département de Biochimie Médicale at Geneva. He was also President of Basic Medicine in Geneva from 1994 to 2000. In 2004 he became the founding Director of a new Department in the Medical Faculty, the Department of Structural Biology and Bioinformatics. He was one of the pioneers of the technique of protein semisynthesis. He was responsible for the first of the so-called anti-HIV "fusion inhibitors" and building on this, he and his colleagues have designed and made a series of semisynthetic and synthetic proteins which are among the most powerful anti-HIV substances currently known. One of them is the first to give full protection against infection in macaques. He is currently adviser to the Netherlands Government on proteomics, to the UN International Trade Centre, and a member of the Geneva government's Council for Regional Economic Development. He has been a Journal Managing Editor, member of many Editorial Boards and has consulted for many major pharmaceutical and biotechnology firms. He has been a co-founder of a number of start-ups. He was a co-founder of the Swiss Institute for Bioinformatics and is Chairman of the Advisory Board of Eclosion, Geneva's new life-sciences incubator. He shared the "Man of the Year 2002" award of the Swiss financial newspaper 'L'agefi'. He has written, co-authored, or edited 6 books and is the author or co-author of 180 published scientific papers, mainly in various fields of protein science.

Session IX : Peptide and Protein Arrays

A WIRING DIAGRAM FOR TYROSINE KINASE-MEDIATED SIGNALING USING PROTEIN MICROARRAYS
Gavin MacBeath received his Ph.D. in Macromolecular and Cellular Structure and Chemistry from The Scripps Research Institute in 1997, training with Prof. Don Hilvert. He then pursued postdoctoral training with Prof. Stuart Schreiber at Harvard University, before accepting a position as the first research fellow at the Bauer Center for Genomics Research in 2000. In July of 2002, Dr. MacBeath began an appointment as assistant professor in the Department of Chemistry and Chemical Biology at Harvard University. Over the past four years, Dr. MacBeath has pioneered the development and use of protein microarrays to pursue a more integrated understanding of protein function, and is currently interfacing protein array technology with high-throughput screening to extend the field of chemical genomics. Dr. MacBeath is also a founding member of Merrimack Pharmaceuticals, an early stage company that unites network biology with drug discovery.

MONITORING AND MANIPULATING THE PROTEOME WITH PEPTIDES AND PEPTOIDS
Thomas Kodadek was born in Chicago, IL in 1959. He received a B.S. in Chemistry from the University of Miami (Fla.) in 1981, a Ph.D. from Stanford University in 1985 and conducted post-doctoral studies with Prof. Bruce Alberts at UCSF from 1985-1987. He was on the Chemistry & Biochemistry faculty of the University of Texas at Austin from 1987-1997. In 1998 he assumed his present position at the University of Texas Southwestern Medical Center in Dallas where he is Professor of Internal Medicine and Molecular Biology. His research interests focus on the mechanism of gene regulation, chemical biology and proteomics.

Session XI: Proteomics and Emerging Technologies

NEW APPROACHES IN PROTEIN SPLICING TO CONTROL PROTEIN STRUCTURE AND FUNCTION
Henning Mootz studied chemistry in Marburg, Germany, and did his Ph.D. in the biochemistry group of Prof. Mohamed Marahiel working on nonribosomal peptide synthesis. He spent a year with Dr. Philippe Marlière at the Institut Pasteur in Paris, France, to explore strategies for the incorporation of non natural amino acids into proteins in vivo. During a postdoctoral stay with Prof. Tom Muir at The Rockefeller University in New York, USA, he developed conditional inteins and became exposed to peptide ligation methodologies. Since 2003 he is head of a junior research group at the Philipps-University of Marburg funded by the Emmy Noether programme of the DFG. The group's research goals center on new approaches for protein engineering and protein semi-synthesis.

CHEMICAL GENETIC ANALYSIS OF CELLULAR SIGNAL TRANSDUCTION
Kevan Shokat received his B.A. in Chemistry from Reed; Ph.D. with Peter Schultz at UC Berkeley; post-doctoral studies with Christopher Goodnow at Stanford University. He moved to Princeton University to become Assistant Professor of Chemistry and Molecular Biology in 1994. At Princeton his group developed novel chemical methods for probing protein kinase signaling cascades using unnatural ATP analogs and uniquely specific protein kinase inhibitors. He is currently Professor of Cellular and Molecular Pharmacalogy at the University of California at San Francisco and Professor of Chemistry at the University of California at Berkeley. Professor Shokat has served as a Pew Scholar in the Biomedical Sciences (1997), a Cottrell Scholar (1998), a Searle Scholar (1998), a Glaxo-Wellcome Scholar in Organic Chemistry (1998), and an Alfred P. Sloan Fellow (1999). He is the recipient of the 2001 Young Investigator Award from the Protein Society and the Eli Lilly Award in Biological Chemistry in 2002 from the American Chemical Society.

Closing Keynote : ENZYMATIC HALOGENATION OF AMINO ACID MOIETIES IN NATURAL PRODUCTS : OXIDATIVE STRATEGIES

Christopher Walsh is the Hamilton Kuhn Professor of Biological Chemistry and Molecular Pharmacology (BCMP) at Harvard Medical School. He has had extensive experience in academic administration, including Chairmanship of the MIT Chemistry Dept (1982-1987) and the HMS Biological Chemistry & Molecular Pharmacology Dept (1987-1995) as well as serving as President and CEO of the Dana Farber Cancer Institute (1992-1995).His research has focused on enzymes and enzyme inhibitors, with recent specialization on antibiotics. He and his group have authored over 600 research papers, three books Enzymatic Reaction Mechanisms (1979); Antibiotics: Origins, Actions, Resistance(2003); Posttranslational Modification of Proteins: Expanding Nature's Inventory (in press). He is a member of the National Academy of Sciences, the Institute of Medicine, and the American Philosophical Society. He has been a consultant to government and academic institutions, including NIGMS, a Trustee of the Whitehead Institute and the Helen Hay Whitney Foundation.