Nucleation effects in peptide foldamers.
Oligomers composed of β(3)-amino acid residues and a mixture of α- and β(3)-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β(3)-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of "αααβ" repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.
Department of Chemistry, New York University, New York, New York 10003, USA.
Anupam
A
Patgiri
Stephen T
ST
Joy
Paramjit S
PS
Arora
D002942:Circular Dichroism; D003903:Deuterium / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D010455:Peptides; D006859:Hydrogen; D003903:Deuterium