Identification of nitroxyl-induced modifications in human platelet proteins using a novel mass spectrometric detection method.

ABSTRACT: Nitroxyl (HNO) exhibits many important pharmacological effects, including inhibition of platelet aggregation, and the HNO donor Angeli's salt has been proposed as a potential therapeutic agent in the treatment of many diseases including heart failure and alcoholism. Despite this, little is known about the mechanism of action of HNO, and its effects are rarely linked to specific protein targets of HNO or to the actual chemical changes that proteins undergo when in contact with HNO. Here we study the presumed major molecular target of HNO within the body: protein thiols. Cysteine-containing tryptic peptides were reacted with HNO, generating the sulfinamide modification and, to a lesser extent, disulfide linkages with no other long lived intermediates or side products. The sulfinamide modific

SUBMITTER: Hoffman MD 

PROVIDER: S-EPMC2689763 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature