【摘 要】
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We develop a generalized,quantitative chemoproteomic platform that can be broadly applicable to the analyses of biorthogonal-chemically engineered PTMs.A key feature of this method is the use of light
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We develop a generalized,quantitative chemoproteomic platform that can be broadly applicable to the analyses of biorthogonal-chemically engineered PTMs.A key feature of this method is the use of light and heavy-labeled Azido biotin reagents with a photocleavable linker,which provides a means not only to site-specifically and quantitatively compare abundances of the biorthogonal-chemically engineered protein PTMs,but also to minimize the false discovery rate of identification.In combination with a blind search tool like TagRecon that enables the identification of all possible mass shifts on a detected peptide sequence,our chemoproteomic platform can also be applied to discover unexpected PTMs labeled by activity-based clickable probes.We have successfully use this strategy in characterization of several previously unknown PTMs,including 4-oxo-2-nonenal(an endogenous lipid electrophile)derived pyrrole-adduction and N-terminal formylation of protein degradants.We foresee that,in combination with new activity-based probes,our chemoproteomics-based strategy can be used to discover more unexpected PTMs with certain functional groups.
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