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Facile terminal functionalization of peptides by protease-catalyzed chemoenzymatic polymerization toward synthesis of polymeric architectures consisting of peptides

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Abstract

Polypeptides are used as building blocks that assemble into polymeric hierarchical architectures with various functionalities based on their amino acid sequences. Chemoenzymatic polymerization using a protease as a catalyst allows us to synthesize peptides with various primary structures in an environmentally benign way. In this work, we performed papain-catalyzed polymerization in the presence of terminal-modifying agents to synthesize peptides modified with a functional group at their N-terminus. Various peptides with a reactive acrylamide group at the N-terminus were synthesized in a one-pot chemoenzymatic reaction with the side groups of the amino acid residues left intact. Acrylamide-modified poly(L-alanine) was used as a macromonomer in a radical copolymerization with N-isopropylacrylamide to give a graft copolymer consisting of poly(L-alanine) side chains.

Graphical abstract: Facile terminal functionalization of peptides by protease-catalyzed chemoenzymatic polymerization toward synthesis of polymeric architectures consisting of peptides

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Publication details

The article was received on 05 Sep 2019, accepted on 01 Oct 2019 and first published on 30 Oct 2019


Article type: Paper
DOI: 10.1039/C9PY01335K
Polym. Chem., 2020, Advance Article
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    Facile terminal functionalization of peptides by protease-catalyzed chemoenzymatic polymerization toward synthesis of polymeric architectures consisting of peptides

    K. Tsuchiya and K. Numata, Polym. Chem., 2020, Advance Article , DOI: 10.1039/C9PY01335K

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