Residue requirements for helical folding in short α/β-peptides: Crystallographic characterization of the 11-helix in an optimized sequence

Margaret A. Schmitt, Soo Hyuk Choi, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticle

103 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)13130-13131
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number38
DOIs
Publication statusPublished - 2005 Sep 28

All Science Journal Classification (ASJC) codes

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

Fingerprint Dive into the research topics of 'Residue requirements for helical folding in short α/β-peptides: Crystallographic characterization of the 11-helix in an optimized sequence'. Together they form a unique fingerprint.

  • Cite this