Conformation Design of a Fully Flexible beta II-Hairpin Analogue

摘要

Isosteric. non-hydrolyzable analogues of secondary-structure elements of peptides are of high current interest in medicinal chemistry and serve as peptidomimetics. Such structural units yield important information on complex structure-activity relationships and are neccessary for a rational design of low-molecular weight, non-peptide pharmaceutical agents. Moreover, such analogues of peptide structures may be important for inducing alpha-helix or beta-turn structures in adjacent peptide sequences. Far less is known about the prerequisites for the induction of beta-sheet structures, in which tertiary interactions play a decisive role. Gellman et al. pointed out that good model systems for studying the formation of beta-hairpin structures arc lacking.