Nucleation effects in peptide foldamers

Anupam Patgiri, Stephen T. Joy, Paramjit S. Arora

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)11495-11502
Number of pages8
JournalJournal of the American Chemical Society
Volume134
Issue number28
DOIs
StatePublished - Jul 18 2012

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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