COLLAGEN MIMETICS

Collagen peptidomimetics have been synthesized as an alternative to na tural collagen. The incorporation of unnatural residues such as peptoi ds in the collagen sequences can demonstrate potent and specific biolo gical activity and enhance the biostability against enzymatic degradat ion. Furthermore, the use of achiral peptoids simplifies synthetic str ategies by reducing racemization problems. The peptoid residue N-isobu tylglycine (Nleu) has been successfully incorporated into a series of collagen mimetics composed of Gly-Pro-Nleu, Gly-Nleu-Pro, and Gly-Nleu -Nleu. The discovery of template-assembled collagen mimetics and metal binding ability has laid the foundation for new opportunities in the design of novel collagen mimetic complexes. This review summarizes the synthesis and integrated biophysical analyses of the structures of th ese collagen mimetics. Solid phase segment condensation techniques hav e been utilized for the synthesis of the single chain and template-ass embled analogues. The characterization of the collagen-like structures has been established by temperature-dependent optical rotation measur ements, CD, NMR spectroscopy, and molecular modelling simulations. (C) 1998 John Wiley & Sons, Inc.