Residue Requirements for Helical Folding in Short α/β-Peptides: Crystallographic Characterization of the 11-Helix in an Optimized Sequence

Publisher Website
Google Scholar
Abstract
Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both α-amino acid and β-amino acid substitution on α/β-peptide helicity. We also report the first X-ray crystal structure of a helical α/β-peptide. We conclude that a certain amount of conformational preorganization in α/β-peptides (via the inclusion of constrained β-amino acids or α,α-disubstituted α-amino acids) is needed to promote helical folding; acyclic β-amino acids and β-branched α-amino acids are tolerated to only a limited extent.

This publication has 14 references indexed in Scilit: