期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 8, 页码 3128-3133出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b00172
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资金
- National Institutes of Health [R01GM460S9, R01GM110535]
- Japan Society for the Promotion of Science
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM046059, R01GM110535, R35GM122483] Funding Source: NIH RePORTER
A new method for cysteine lysine cross-linking in peptides and proteins using palladium oxidative addition complexes is presented. First, a biarylphosphine-supported palladium reagent is used to transfer an aryl group bearing an O-phenyl carbamate substituent to a cysteine residue. Next, this carbamate undergoes chemoselective acyl substitution by a proximal lysine to form a cross-link. The linkage so formed is stable toward acid, base, oxygen, and external thiol nucleophiles. This method was applied to cross-link cysteine with nearby lysines in sortase A*. Furthermore, we used this method for the intermolecular cross-linking between a peptide and a protein based on the p53-MDM2 interaction. These studies demonstrate the potential for palladium-mediated methods to serve as a platform for the development of future cross-linking techniques for peptides and proteins with natural amino acid residues.
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