A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate

Ross N. Chapman, Gianluca Dimartino, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

Herein we describe a strategy for the preparation of artificial α-helices involving replacement of one of the main-chain hydrogen bonds with a covalent linkage. To mimic the C=O⋯H-N hydrogen bond as closely as possible, we envisioned a covalent bond of the type C=X-Y-N, where X and Y are two carbon atoms connected through an olefin metathesis reaction. Our results demonstrate that the replacement of a hydrogen bond between the i and i + 4 residues at the N-terminus of a short peptide with a carbon-carbon bond results in a highly stable constrained α-helix at physiological conditions as indicated by CD and NMR spectroscopies. The advantage of this strategy is that it allows access to short α-helices with strict preservation of molecular recognition surfaces required for biomolecular interactions.

Original languageEnglish (US)
Pages (from-to)12252-12253
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number39
DOIs
StatePublished - Oct 6 2004

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Hydrogen
Hydrogen bonds
Carbon
Molecular recognition
Covalent bonds
Alkenes
Peptides
Nuclear magnetic resonance spectroscopy
Olefins
Magnetic Resonance Spectroscopy
Atoms
hydroxide ion

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate. / Chapman, Ross N.; Dimartino, Gianluca; Arora, Paramjit.

In: Journal of the American Chemical Society, Vol. 126, No. 39, 06.10.2004, p. 12252-12253.

Research output: Contribution to journalArticle

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