ArticleNature communications2019
Enzyme-mimetic self-catalyzed polymerization of polypeptide helices.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 70 citations in OpenAlex.
- Proton Transfer Shuttle Mediated Dormant-Active Balance for Accelerated and Controlled Polymerization of N-Carboxyanhydrides.Angewandte Chemie (International ed. in English) · 2026Article
- Integrating synthetic polypeptides with innovative material forming techniques for advanced biomedical applications.Journal of nanobiotechnology · 2025Review
- A nanoscale MOF-based heterogeneous catalytic system for the polymerization of N-carboxyanhydrides enables direct routes toward both polypeptides and related hybrid materials.Nature communications · 2023Article
- Open-air synthesis of oligo(ethylene glycol)-functionalized polypeptides from non-purifiedBiomaterials science · 2021Article
- Accelerated polymerization of N-carboxyanhydrides catalyzed by crown ether.Nature communications · 2021Article
- Amphiphilic Nucleobase-Containing Polypeptide Copolymers-Synthesis and Self-Assembly.Polymers · 2020Article
- Helical polymers for biological and medical applications.Nature reviews. Chemistry · 2020Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.