Oxidation-induced generation of a mild electrophile for proximity-enhanced protein-protein crosslinking

X. Shang; Y. Chen; N. Wang; W. Niu; J. Guo

doi:10.1039/c8cc01639a

Oxidation-induced generation of a mild electrophile for proximity-enhanced protein-protein crosslinking

X. Shang, Y. Chen, N. Wang, W. Niu, J. Guo

Chemistry

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

6 Scopus citations

Abstract

We report a strategy to introduce a reactive electrophile into proteins through the conversion of a chemically inert group into a bioreactive group in response to an inducer molecule. This strategy was demonstrated by oxidation-induced and proximity-enhanced protein-protein crosslinking in the presence of a large excess of free nucleophile.

Original language	English (US)
Pages (from-to)	4172-4175
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	33
DOIs	https://doi.org/10.1039/c8cc01639a
State	Published - 2018

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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title = "Oxidation-induced generation of a mild electrophile for proximity-enhanced protein-protein crosslinking",

abstract = "We report a strategy to introduce a reactive electrophile into proteins through the conversion of a chemically inert group into a bioreactive group in response to an inducer molecule. This strategy was demonstrated by oxidation-induced and proximity-enhanced protein-protein crosslinking in the presence of a large excess of free nucleophile.",

author = "X. Shang and Y. Chen and N. Wang and W. Niu and J. Guo",

note = "Funding Information: This study was supported by the National Institute of Health (grant 1R01AI111862 to J. G. and W. N.), National Science Foundation (grant 1553041 to J. G.). The authors thank Drs Sophie Alvarez and Mike Naldrett (Proteomics and Meta-bolomics Facility) for mass spectrometry analysis. Funding Information: This study was supported by the National Institute of Health (grant 1R01AI111862 to J. G. and W. N.), National Science Foundation (grant 1553041 to J. G.). Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",

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T1 - Oxidation-induced generation of a mild electrophile for proximity-enhanced protein-protein crosslinking

AU - Shang, X.

AU - Chen, Y.

AU - Wang, N.

AU - Niu, W.

AU - Guo, J.

N1 - Funding Information: This study was supported by the National Institute of Health (grant 1R01AI111862 to J. G. and W. N.), National Science Foundation (grant 1553041 to J. G.). The authors thank Drs Sophie Alvarez and Mike Naldrett (Proteomics and Meta-bolomics Facility) for mass spectrometry analysis. Funding Information: This study was supported by the National Institute of Health (grant 1R01AI111862 to J. G. and W. N.), National Science Foundation (grant 1553041 to J. G.). Publisher Copyright: © 2018 The Royal Society of Chemistry.

PY - 2018

Y1 - 2018

N2 - We report a strategy to introduce a reactive electrophile into proteins through the conversion of a chemically inert group into a bioreactive group in response to an inducer molecule. This strategy was demonstrated by oxidation-induced and proximity-enhanced protein-protein crosslinking in the presence of a large excess of free nucleophile.

AB - We report a strategy to introduce a reactive electrophile into proteins through the conversion of a chemically inert group into a bioreactive group in response to an inducer molecule. This strategy was demonstrated by oxidation-induced and proximity-enhanced protein-protein crosslinking in the presence of a large excess of free nucleophile.

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DO - 10.1039/c8cc01639a

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EP - 4175

JO - Chemical Communications

JF - Chemical Communications

IS - 33

ER -

Oxidation-induced generation of a mild electrophile for proximity-enhanced protein-protein crosslinking

Abstract

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