title: Conformational constraints: nonpeptide beta-turn mimics.
abstract: The beta-turn, which has also been referred to as the beta-bend, beta-loop or reverse turn, has been implicated as an important site for molecular recognition in many biologically active peptides and in globular proteins. This small secondary structure therefore makes an attractive target for mimicry by a conformational constraint, because a peptide which is constrained in a biologically active conformation can display a number of advantages over the parent substrate. The less peptide-like such a constraint is, the more potential there is to maximize these advantages. A decade has passed since the first (and highly successful) attempt to mimic the beta-turn with a nonpeptide conformational constraint was disclosed by Freidinger et al. (1980). Since this report, rapidly growing interest in the field of nonpeptide beta-turn mimics has seen a variety of experimental approaches and a mixed bag of results. It is attempted in this review, not only to summarize and critically analyse these approaches, but also to touch on the complexities associated with the conformational mimicry of such a diverse structure as the beta-turn.
authors.affiliation: School of Pharmaceutical Chemistry, Victorian College of Pharmacy Ltd., Parkville, Australia.
authors.forename: J B
authors.initials: JB
authors.lastname: Ball
authors.forename: P F
authors.initials: PF
authors.lastname: Alewood
mesh_terms: D015195:Drug Design; D015394:Molecular Structure; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism
chemical_list: D010455:Peptides; D011956:Receptors, Cell Surface