Proteomic analysis of peptides tagged with dimedone and related probes.

ABSTRACT: Owing to its labile nature, a new role for cysteine sulfenic acid (-SOH) modification has emerged. This oxidative modification modulates protein function by acting as a redox switch during cellular signaling. The identification of proteins that undergo this modification represents a methodological challenge, and its resolution remains a matter of current interest. The development of strategies to chemically modify cysteinyl-containing peptides for liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis has increased significantly within the past decade. The method of choice to selectively label sulfenic acid is based on the use of dimedone or its derivatives. For these chemical probes to be effective on a proteome-wide level, their reactivity toward -SOH must be high to ensure r

SUBMITTER: Martinez-Acedo P 

PROVIDER: S-EPMC4070747 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature