One ofthe major drivers in biological research is the establishment ofstructures and functions of the 50,000 or so proteins in our bodies. Each has a characteristic- dimensional structure, highly "ordered" yet "disordered"! This structure is essential for a protein's function and, significantly, it must be sustained in the competitive and complex environment of the living cell. It is now being recognised that when a cell loses control, proteins can se- assemble into more complex supermolecular structures such as the amyloid fibres and plaques associated with the pathogenesis of prion (CJD) or age-related (Alzheimer's) diseases. This is a pointer to the wider significance of the self-assembling properties of polypeptides. It has been long known that, in silk, polypeptides are assembled into- sheet structures which impart on the material its highly exploitable properties of flexibility combined with high tensile strength. But only now emerging is the recognition that peptides can Self-assemble into a wide variety of non-protein-like structures, including fibrils, fibres, tubules, sheets and monolayers. These are exciting observations and, more so, the potential for materials and medical exploitations is so wide ranging that over 80 scientists from Europe, USA, Japan and Israel. met 1-6 July 1999 in Crete, to discuss the wide-ranging implications of these novel developments. There was a spirit of excitement about the workshop indicative of an important new endeavor. The emerging perception is that of a new class of materials set to become commercially viable early in the 21st century.

InhaltsangabeForeword. 1. Exploiting peptide self-assembly to engineer novel biopolymers: tapes, ribbons, fibrils and fibres; A. Aggeli, et al. 2. Ribbon-like lamellar structures from chain-folded polypeptides; E.D.T. Atkins. 3. Design of self-assembling peptides as catalyst mimetics using combintatorial libraries; S.E. Blondelle, et al. 4. Thermodynamics of protein-protein and peptide interactions; A. Cooper. 5. The mechanism of amyloid formation and its links to human disease and biological evolution; C.M. Dobson. 6. Transgenic plants for large scale production of peptides and proteins; K. Düring. 7. Assembly modulation of channel-forming peptides; S. Futaki. 8. Molecular casting of infectious amyloids, inorganic and organic replication: nucleation, conformational change and self-assembly; D.C. Gajdusek. 9. Structure and stabilisation of self-assembling peptide filaments; N.J. Gay, et al. 10. Designed combinatorial libraries of novel amyloid-like proteins; M.H. Hecht, et al. 11. Design of synthetic branched-chain polymeric polypeptides for targeting/delivering bioactive molecules; F. Hudecz. 12. Amyloid-like fibrils from a peptide-analogue of the central domain of silkmoth chorion proteins; V.A. Iconomidou, S.J. Hamodrakas. 13. Amyloidogenesis of islet amyloid polypetide (IAPP); A. Kapurniotu. 14. Engineering self-assembly of peptides by Amphiphilic 2D motifs: alpha- to -beta transitions of Peptides; H. Mihara, et al. 15. Model signal peptides: probes of molecular interactions during protein secretion; A. Miller, et al.16. Structure, folding and assembly of adenovirus fibers; A. Mitraki, et al. 17. Solving the structure of collagen; A. Rich. 18. Disulfide bond based on self-assembly of peptides leading to spheroidal cyclic trimers; M. Royo, et al. 19. A new circular helicoid-type sequential oligopeptide carrier for assembling multiple antigenic peptides; M. Sakarellos-Daitsiotis, et al. 20. Molecular recognition in the membrane: role in the folding of membrane proteins; Y. Shai. 21. Novel peptide nucleic acids with improved solubility and DNA-binding ability; M. Sisido, M. Kuwahara. 22. Chiral lipid tubules; M.S. Spector, et al. 23. &Dgr; Tt-Mechanism in the design of self-assembling structures; D.W. Urry, et al. Self-assembling peptide systems in biology and biomedical engineering; S. Zhang, M. Altman. Index.