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An efficient and robust oxidative elimination of cysteine to dehydroalanine has been discovered. The reaction is induced by O-mesitylenesulfonylhydroxylamine (MSH) and is compatible with methionine. The key elimination has been executed on protein surfaces and allows ready access to different post-translationally modified proteins through conjugate addition of sulfur nucleophiles to dehydroalanine. Treatment of the resulting thioether with MSH results in regeneration of dehydroalanine, allowing a "functional switch" by subsequent addition of a different thiol.

Original publication

DOI

10.1021/ja800800p

Type

Journal article

Journal

J Am Chem Soc

Publication Date

16/04/2008

Volume

130

Pages

5052 - 5053

Keywords

Alanine, Alkylation, Cysteine, Models, Molecular, Molecular Structure, Protein Processing, Post-Translational, Proteins, Spectrometry, Mass, Electrospray Ionization, Surface Properties