Exposure of a monoclonal antibody, IgG1, to UV-light leads to protein dithiohemiacetal and thioether cross-links: a role for thiyl radicals?
Chem Res Toxicol
; 23(8): 1310-2, 2010 Aug 16.
Article
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| MEDLINE
| ID: mdl-20604533
ABSTRACT
Recently, we characterized a thiyl 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.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Compuestos de Sulfhidrilo
/
Sulfuros
/
Rayos Ultravioleta
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Inmunoglobulina G
Idioma:
En
Revista:
Chem Res Toxicol
Asunto de la revista:
TOXICOLOGIA
Año:
2010
Tipo del documento:
Article
País de afiliación:
Estados Unidos