Chemistry - A European Journal · 1999 · 12 citations · 0 references
PharmacyChemistryMedicinal ChemistryDrug DesignDrug DiscoveryStructural BiologyConformational AnalysisPeptide ChemistryPeptide Drug DiscoveryPeptidomimetic DesignProtein ConformationSecondary StructureBeta Turn ConformationBeta-turn FormationCyclic PeptidomimeticsMacrocyclic PeptidesMacrocyclic PeptidomimeticsPeptide Structure AnalysisPeptidomimetic MacrocyclesStructure-based Peptidomimetics
Theβ-turn peptidomimics 1 were designed to have “turn–extended-pseudo-turn” conformations similar to some cyclic hexapeptides, and it was proposed that n=1 would be ideal for this. NMR and CD studies, interfaced with molecular simulations, verified that the molecules indeed prefer β-turn conformations in the dipeptide fragment, and that such conformations were most easily attained when n=1. The turn type adopted by the dipeptide fragment was shown to be close to an ideal type I β-turn.