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作 者:Tong Zhu Lu Song Ruifeng Li Bian Wu
机构地区:[1]CAS Key Laboratory of Microbial Physiological and Metabolic Engineering,State Key Laboratory of Microbial Resources,Institute of Microbiology,Chinese Academy of Sciences,Beijing 100101,China [2]University of Chinese Academy of Sciences,Beijing 100101,China [3]State Key Laboratory of Transducer Technology,Chinese Academy of Sciences,Beijing 100101,China
出 处:《Chinese Chemical Letters》2018年第7期1116-1118,共3页中国化学快报(英文版)
基 金:supported by the National Natural Science Foundation of China(No.31601412);the 100 Talent Program grant and Biological Resources Service Network Initiative(No.ZSYS-012);grant from the Chinese Academy of Sciences(No.SKT1604)
摘 要:Directed peptides C-terminal modification enabled by the engineered biomolecular catalyst-peptide amidase 12 B has been achieved via computational protein engineering. The engineered enzyme exhibits great promising potential in the C-terminal modification of opioid peptides using prop-2-yn-1-amine(PYA) or prop-2-en-l-amine(PEA) as the nucleophile. A variety of opioid peptides could be readily functionalized at the C-terminal chain in high yield in a mild and selective manner. Notably, modified opioid peptides bearing alkynyl moiety could be further functionalized through well-established click reaction.Directed peptides C-terminal modification enabled by the engineered biomolecular catalyst-peptide amidase 12 B has been achieved via computational protein engineering. The engineered enzyme exhibits great promising potential in the C-terminal modification of opioid peptides using prop-2-yn-1-amine(PYA) or prop-2-en-l-amine(PEA) as the nucleophile. A variety of opioid peptides could be readily functionalized at the C-terminal chain in high yield in a mild and selective manner. Notably, modified opioid peptides bearing alkynyl moiety could be further functionalized through well-established click reaction.
关 键 词:Peptide amidase Opioid peptides C-terminal modification Click reaction FUNCTIONALIZATION
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