Extent of Helical Induction Caused by Introducing α-Aminoisobutyric Acid into an Oligovaline Sequence

摘要

The preferred conformations of a dodecapeptide composed of l-valine (l-Val) and α-aminoisobutyric acid (Aib) residues, Boc-(l-Val-l-Val-Aib)_(4)-OMe (3 ), were analyzed in solution and in the crystalline state. Peptide 3 predominantly folded into a mixture of α- and 3_(10)-(P ) helical structures in solution and a (P ) α helix in the crystalline state.