Impact of Backbone Pattern and Residue Substitution on Helicity in α/β/γ-Peptides.

ABSTRACT: We have evaluated the impact of changes in the chemical structure of peptidic oligomers containing α-, β-, and γ-amino acid residues (α/β/γ-peptides) on the propensities of these oligomers to adopt helical conformations in aqueous and alcoholic solutions. These studies were inspired by our previous discovery that α/β/γ-peptides containing a regular αγααβα hexad repeat adopt an α-helix-like conformation in which the β and γ residues are aligned in a stripe along one side, and the remainder of the helix surface is defined by the α residues. This helix was found to be most stable when the β and γ residues were rigidified with specific cyclic constraints. Relaxation of the β residue constraints caused profound conformational destabilization, but relaxation of the γ residue constraints led to o

SUBMITTER: Shin YH 

PROVIDER: S-EPMC5986291 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature