Differential Effects of β³ - versus β² -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.

ABSTRACT: Oligomers containing α- and β-amino acid residues (α/β-peptides) have been shown to mimic the α-helical conformation of conventional peptides when the unnatural residues are derived from β³ -amino acids or cyclic β-amino acids, but the impact of incorporating β² residues has received little attention. The effects of β² residues on the conformation and recognition behavior of α/β-peptides that mimic an isolated α-helix were investigated. This effort has focused on 26-mers based on the Bim BH3 domain; a set of isomers with identical α/β backbones that differ only in the placement of certain side chains along the backbone (β³ vs. β² substitution) was compared. Circular dichroism data suggest that β² residues can be helix-destab

SUBMITTER: Eddinger GA 

PROVIDER: S-EPMC6330212 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature