Highly efficient "grafting from" an α-helical polypeptide backbone by atom transfer radical polymerization
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Updated: Jun 7, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Jianxun Ding1, Chunsheng Xiao, Zhaohui Tang
1Key Laboratory of Polymer Ecomaterials, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, P. R. China.
Abstract:
Because of their favorable biodegradability, biocompatibility, regular secondary structures, and stimuli-responsiveness, synthetic polypeptides have attracted more and more attention in the biomedical material field. In this work, a novel thermo-responsive graft polypeptide, poly(L-glutamate)-graft-poly(2-(2-methoxyethoxy)ethyl methacrylate) (PLG-g-PMEO₂ MA), is prepared through a combination of ring-opening polymerization and atom transfer radical polymerization. The structure of PLG-g-PMEO₂ MA is confirmed by FT-IR, ¹H NMR, and GPC analyses. The phase transition temperature of PLG-g-PMEO₂ MA is adjustable by varying the NaCl concentration in aqueous solution. PLG-g-PMEO₂ MA adopts α-helical conformations both in aqueous solution at 25 and 60 °C and even in the solid state. In addition, PLG-g-PMEO₂ MA forms stimuli-responsive micelles with an α-helical core and a thermo-responsive shell in water.
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