Enzyme-mimetic self-catalyzed polymerization of polypeptide helices

Ziyuan Song, Hailin Fu, Ryan Baumgartner, Lingyang Zhu, Kuo-Chih Shih, Yingchun Xia, Xuetao Zheng, Lichen Yin, Christophe Chipot (), Yao Lin () and Jianjun Cheng ()
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Ziyuan Song: University of Illinois at Urbana-Champaign
Hailin Fu: University of Connecticut
Ryan Baumgartner: University of Illinois at Urbana-Champaign
Lingyang Zhu: University of Illinois at Urbana-Champaign
Kuo-Chih Shih: University of Connecticut
Yingchun Xia: University of Illinois at Urbana-Champaign
Xuetao Zheng: University of Illinois at Urbana-Champaign
Lichen Yin: Soochow University
Christophe Chipot: University of Illinois at Urbana-Champaign
Yao Lin: University of Connecticut
Jianjun Cheng: University of Illinois at Urbana-Champaign

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract Enzymes provide optimal three-dimensional structures for substrate binding and the subsequent accelerated reaction. Such folding-dependent catalytic behaviors, however, are seldom mechanistically explored with reduced structural complexity. Here, we demonstrate that the α-helix, a much simpler structural motif of enzyme, can facilitate its own growth through the self-catalyzed polymerization of N-carboxyanhydride (NCA) in dichloromethane. The reversible binding between the N terminus of α-helical polypeptides and NCAs promotes rate acceleration of the subsequent ring-opening reaction. A two-stage, Michaelis–Menten-type kinetic model is proposed by considering the binding and reaction between the propagating helical chains and the monomers, and is successfully utilized to predict the molecular weights and molecular-weight distributions of the resulting polymers. This work elucidates the mechanism of helix-induced, enzyme-mimetic catalysis, emphasizes the importance of solvent choice in the discovery of new reaction type, and provides a route for rapid production of well-defined synthetic polypeptides by taking advantage of self-accelerated ring-opening polymerizations.

Date: 2019
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DOI: 10.1038/s41467-019-13502-w

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