Allyl sulfides are privileged substrates in aqueous cross-metathesis: application to site-selective protein modification.
Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported.
Lin
Yuya A
YA
Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, U.K.
Chalker
Justin M
JM
Floyd
Nicola
N
Bernardes
Gonçalo J L
GJ
Davis
Benjamin G
BG
D000498:Allyl Compounds / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry*; D003545:Cysteine / Q000031:analogs & derivatives / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005959:Glucosidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008715:Methionine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D020860:Subtilisin / Q000737:chemistry; D013440:Sulfides / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D000498:Allyl Compounds; D001426:Bacterial Proteins; D013440:Sulfides; D014867:Water; C038491:allyl sulfide; C065299:S-allylcysteine; D008715:Methionine; D005959:Glucosidases; C104851:Sulfolobus solfataricus beta-glycosidase; D020860:Subtilisin; D003545:Cysteine