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Peptide Modification via N-Terminal-Residue-Directed γ-C(sp3)-H Arylation
Zhen-Lin Hou1, Feipeng Yuan1, Bo Yao1,2
1MOE Key Laboratory of Cluster Science, Beijing Key Laboratory of Photoelectronic-Electrophotonic Conversion Materials, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 102488, P. R. China.
Abstract:
Postassembly modification of peptides via C(sp3)-H functionalization provides an efficient way to prepare functionalized peptides for biological study and pharmaceutical development. In this work, we developed a new method for γ-C(sp3)-H functionalization of aliphatic side chains of N-terminus-unprotected peptides. With the N-terminal residues as directing groups, a wide range of di-, tri-, tetra-, and pentapeptides underwent C-H arylation of the residues (Val, Ile, Tle) at the +2 position from the N-terminus.
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