期刊
ORGANIC LETTERS
卷 21, 期 1, 页码 104-108出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.8b03536
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资金
- Nottingham Trent University (NTU)
- University Rovira i Virgili, Spain
New methods for peptide modification are in high demand in drug discovery, chemical biology, and materials chemistry; methods that modify natural peptides are particularly attractive. A Pd-catalyzed, C-H functionalization protocol for the olefination of phenylalanine residues in peptides is reported, which is compatible with common amino acid protecting groups, and the scope of the styrene reaction partner is broad. Bidentate coordination of the peptide to the catalyst appears crucial for the success of the reaction.
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