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Issue 39, 2011
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Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

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Abstract

Covalent side-chain cross-linking has been shown to be a viable strategy to control peptide folding. We report here that an oxime side-chain linkage can elicit α-helical folds from peptides in aqueous solution. The bio-orthogonal bridge is formed rapidly under neutral buffered conditions, and the resulting cyclic oximes are capable of dynamic covalent exchange.

Graphical abstract: Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

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Article information


Submitted
08 Apr 2011
Accepted
02 Jun 2011
First published
20 Jun 2011

Chem. Commun., 2011,47, 10915-10917
Article type
Communication

Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

C. M. Haney, M. T. Loch and W. S. Horne, Chem. Commun., 2011, 47, 10915
DOI: 10.1039/C1CC12010G

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