Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: versatile and switchable access to functionalized proteins.
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.
Bernardes
Gonçalo J L
GJ
Chemistry Research Laboratory, Dept. of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Chalker
Justin M
JM
Errey
James C
JC
Davis
Benjamin G
BG
D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry; D000478:Alkylation; D003545:Cysteine / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D013499:Surface Properties
D011506:Proteins; C015102:dehydroalanine; D003545:Cysteine; D000409:Alanine