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. Copyright
Bernardes, Goncalo J. L.,Chalker, Justin M.,Errey, James C.,Davis, Benjamin G.
p. 5052 - 5053
(2008/10/09)
Pleuromutilins
Compounds of formula I STR1 wherein R1 and R2 are the same or different and each represent hydrogen, alkyl, alkenyl, cycloalkyl, aryl or aralkyl are produced by a new environmentally acceptable process.
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(2008/06/13)
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