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| Enzymatic clickable functionalization of peptides via computationally engineered peptide amidase |
| Tong Zhua,b, Lu Songa,c, Ruifeng Lia,b, Bian Wua |
a 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;
b University of Chinese Academy of Sciences, Beijing 100101, China;
c State Key Laboratory of Transducer Technology, Chinese Academy of Sciences, Beijing 100101, China |
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| Guide The computationally engineered peptide amidase exhibits great promising potential in the C-terminal modification of peptides using prop-2-yn-1-amine (PYA) or prop-2-en-1-amine (PEA) as the nucleophile. Subsequently, modified peptides could be further functionalized via click reaction without elaborate isolation of the intermediate. |
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Abstract Directed peptides C-terminal modification enabled by the engineered biomolecular catalyst-peptide amidase 12B 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-1-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.
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Received: 05 February 2018
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| Fund:This work is 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) and grant from the Chinese Academy of Sciences (No. SKT1604). |
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Corresponding Authors:
Bian Wu, wub@im.ac.cn
E-mail: wub@im.ac.cn
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