Reversible redox reconfiguration of secondary structures in a designed peptide

Xiaojian Wang; Irina Bergenfeld; Paramjit S. Arora; James W. Canary

doi:10.1002/anie.201206009

Reversible redox reconfiguration of secondary structures in a designed peptide

Xiaojian Wang, Irina Bergenfeld, Paramjit S. Arora, James W. Canary

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Secondary structures are critical regulators of protein structure and function. Switchable peptides that can adopt multiple defined conformations in response to stimuli are attractive model systems for the study of protein folding and misfolding. A peptide is presented that can be reversibly reconfigured between an α-helical monomer and a β-sheet aggregate upon one-electron oxidation and reduction in the presence of Cu ^I/Cu^II.

Original language	English (US)
Pages (from-to)	12099-12101
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	48
DOIs	https://doi.org/10.1002/anie.201206009
State	Published - Nov 26 2012

Keywords

peptide switches
peptides
protein structures
redox chemistry

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201206009

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abstract = "Secondary structures are critical regulators of protein structure and function. Switchable peptides that can adopt multiple defined conformations in response to stimuli are attractive model systems for the study of protein folding and misfolding. A peptide is presented that can be reversibly reconfigured between an α-helical monomer and a β-sheet aggregate upon one-electron oxidation and reduction in the presence of Cu I/CuII.",

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author = "Xiaojian Wang and Irina Bergenfeld and Arora, {Paramjit S.} and Canary, {James W.}",

year = "2012",

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AU - Bergenfeld, Irina

AU - Arora, Paramjit S.

AU - Canary, James W.

PY - 2012/11/26

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AB - Secondary structures are critical regulators of protein structure and function. Switchable peptides that can adopt multiple defined conformations in response to stimuli are attractive model systems for the study of protein folding and misfolding. A peptide is presented that can be reversibly reconfigured between an α-helical monomer and a β-sheet aggregate upon one-electron oxidation and reduction in the presence of Cu I/CuII.

KW - peptide switches

KW - peptides

KW - protein structures

KW - redox chemistry

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Reversible redox reconfiguration of secondary structures in a designed peptide

Abstract

Keywords

ASJC Scopus subject areas

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