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Issue 10, 2013
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Radical induced disulfide bond cleavage within peptides via ultraviolet irradiation of an electrospray plume

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Abstract

Radical induced disulfide bond cleavage in peptides was demonstrated by ultraviolet (UV) radiation of the electrospray ionization (ESI) plume using a low pressure mercury (LP-Hg) lamp. Tandem mass spectrometry and accurate mass measurements confirmed that the primary reaction products were due to disulfide bond cleavage to form thiol (–SH) and sulfinyl radical (–SO˙). Mechanistic studies showed that the 185 nm emission from a LP-Hg lamp was responsible for UV photolysis of atmospheric O2, which further initiated secondary radical formation and subsequent disulfide bond cleavage by radical attack. The radical induced disulfide bond cleavage was found to be analytically useful in providing rich sequence information for naturally occurring peptides containing intrachain disulfide bonds. The utility of this method was also demonstrated for facile disulfide peptide identification and characterization from protein digests.

Graphical abstract: Radical induced disulfide bond cleavage within peptides via ultraviolet irradiation of an electrospray plume

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Supplementary files

Article information


Submitted
11 Feb 2013
Accepted
21 Mar 2013
First published
21 Mar 2013

Analyst, 2013,138, 2840-2846
Article type
Paper

Radical induced disulfide bond cleavage within peptides via ultraviolet irradiation of an electrospray plume

C. A. Stinson and Y. Xia, Analyst, 2013, 138, 2840
DOI: 10.1039/C3AN00303E

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