ArticleProceedings of the National Academy of Sciences of the United States of America2018
Conformational entropy of a single peptide controlled under force governs protease recognition and catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. 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.
- Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach.iScience · 2026Article
- Mechanism of Cationic Peptide-Induced Assembly of Gold Nanoparticles: Modulation of Electrostatic Repulsion.Aggregate (Hoboken, N.J.) · 2025Article
- PepFun: Open Source Protocols for Peptide-Related Computational Analysis.Molecules (Basel, Switzerland) · 2021Article
- An automated protocol for modelling peptide substrates to proteases.BMC bioinformatics · 2020Article
- Structural basis of mammalian mucin processing by the human gut O-glycopeptidase OgpA from Akkermansia muciniphila.Nature communications · 2020Article
- The bacterial metalloprotease NleD selectively cleaves mitogen-activated protein kinases that have high flexibility in their activation loop.The Journal of biological chemistry · 2020Article
- Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin.The Journal of biological chemistry · 2019Article
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Authors and funding
3 authors.
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Abstract
An immense repertoire of protein chemical modifications catalyzed by enzymes is available as proteomics data. Quantifying the impact of the conformational dynamics of the modified peptide remains challenging to understand the decisive kinetics and amino acid sequence specificity of these enzymatic reactions in vivo, because the target peptide must be disordered to accommodate the specific enzyme-binding site. Here, we were able to control the conformation of a single-molecule peptide chain by applying mechanical force to activate and monitor its specific cleavage by a model protease. We found that the conformational entropy impacts the reaction in two distinct ways. First, the flexibility and accessibility of the substrate peptide greatly increase upon mechanical unfolding. Second, the conformational sampling of the disordered peptide drives the specific recognition, revealing force-dependent reaction kinetics. These results support a mechanism of peptide recognition based on conformational selection from an ensemble that we were able to quantify with a torsional free-energy model. Our approach can be used to predict how entropy affects site-specific modifications of proteins and prompts conformational and mechanical selectivity.
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