Highlight

Enzyme-mimetic self-catalyzed polymerization of polypeptide helices. 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. Nature Communications, 2019.

Recent publications


The Binding of Palonosetron and Other Antiemetic Drugs to the Serotonin 5-HT3 Receptor
Eleftherios Zarkadas; Hong Zhang; Wensheng Cai; Gregory Effantin; Jonathan Perot; Jacques Neyton; Christophe Chipot; Guy Schoehn; Francois Dehez; Hugues Nury;
Structure (2020) 28: 1131-1140
Annexin-V stabilizes membrane defects by inducing lipid phase transition
Yi-Chih Lin; Christophe Chipot; Simon Scheuring;
Nature Communications (2020) 11:230
Scalable molecular dynamics on CPU and GPU architectures with NAMD
James C. Phillips; David J. Hardy; Julio D. C. Maia; John E. Stone; Joao V. Ribeiro; Rafael C. Bernardi; Ronak Buch; Giacomo Fiorin; Jerome Henin; Wei Jiang; Ryan McGreevy; Marcelo C. R. Melo; Brian K. Radak; Robert D. Skeel; Abhishek Singharoy; Yi Wang; Benoit Roux; Aleksei Aksimentiev; Zaida Luthey-Schulten; Laxmikant V. Kale; Klaus Schulten; Christophe Chipot; Emad Tajkhorshid;
The Journal of Chemical Physics (2020) 153 (4): 044130

News

- Renewal of the Laboratoire International Associé CNRS-University of Illinois at Urbana-Champaign on November 2016
- An update of ParseFEP is available in the latest version of VMD.
- 新的分子动力学讲义 (Dissemination).
 

Contact

Laboratoire International Associé
CNRS-UIUC
Unité mixte de recherche n°7019
Université de Lorraine, B.P. 70239
54506 Vandoeuvre-lès-Nancy Cedex, France
 
Phone: +33(0)3 72 74 50 75
 
How to reach us