Journal
CHEMICAL RESEARCH IN TOXICOLOGY
Volume 23, Issue 8, Pages 1310-1312Publisher
AMER CHEMICAL SOC
DOI: 10.1021/tx100193b
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Funding
- Amgen Inc.
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Recently, we characterized a allyl radical-dependent mechanism for the photolytic conversion of a disulfide bond in a model peptide into dithiohemiacetal and subsequently into thioether (Mozziconacci et al. (2010) J. Phys. Chem B 114, 3668-3688). This mechanism is of potential relevance for the photodegradation of disulfide-containing proteins, which may be a problem for the production and formulation of diagnostic and therapeutic protein pharmaceuticals. In this Rapid Report, we show that similar products are also formed when an antibody (IgG1) is subjected to photoirradiation at 253.7 nm, suggesting the involvement of thiyl radicals also in these processes. A series of dithiohemiacetal and thioether cross-links were identified in photoirradiated IgG1 through HPLC-MS/MS analysis.
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