ArticleACS omega2026
Collagen's Triple Helix Reduces the Susceptibility to Base-Catalyzed Hydrolysis.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
2 authors.
Funding
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Abstract
Collagen is the most abundant structural protein in mammals. As the primary component of tendons, ligaments, and other connective tissues, it has to withstand extreme forces. Base-catalyzed peptide hydrolysis was recently shown to be greatly accelerated by mechanical force. This puts collagen at risk of degradation under physiological loads, yet collagen is known to be remarkably stable. Using hybrid quantum mechanics/molecular mechanics (QM/MM) simulations, we investigated the hydrolysis reaction within the complex chemical environment of a collagen triple helix. We demonstrate that the unique triple-helical structure increases the reaction barrier for base-catalyzed hydrolysis compared to a single peptide chain. Our results can explain why collagen mechanical failure proceeds through homolytic bond rupture and mechanoradical formation.
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Registered trials
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 Socratic graph.