Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins.

ABSTRACT: Cysteine sulfenic acid formation in proteins results from the oxidative modification of susceptible cysteine residues by hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. This species represents a biologically significant modification occurring during oxidant signaling or oxidative stress, and it can modulate protein function. Most methods to identify such oxidatively modified proteins rely on monitoring the loss of one or more thiol group(s) or on selective labeling of nascent thiol groups following reduction of oxidized proteins. Our previous work reported the direct labeling of these chemically distinct modifications with a dimedone analogue, 1,3-cyclohexadione, to which a linker and functional group (an alcohol) had been added; further addition of a fluorescent isatoic acid o

SUBMITTER: Poole LB 

PROVIDER: S-EPMC2526167 | biostudies-literature | 2007 Nov-Dec

REPOSITORIES: biostudies-literature