ArticleJournal of enzyme inhibition and medicinal chemistry2026
Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics.
Article in Journal of enzyme inhibition and medicinal chemistry, 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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Abstract
Cathepsin K (CatK), a promising therapeutic target for bone-related diseases, uniquely unfolds triple-helical collagen and digests tropocollagen into soluble peptides in the presence of chondroitin 4-sulphate (C4-S). However, the molecular mechanism of CatK-mediated collagenolysis remains poorly understood, hindering the rational design of selective inhibitors. In this study, we performed microsecond-scale molecular dynamics simulations of a fully solvated ternary complex comprising the CatK dimer, tropocollagen segment, and C4-S, to indicate the structural and dynamical basis of tropocollagen unwinding. The process was initiated by the progressive disruption of six key inter-chain hydrogen bonds within the tropocollagen. C4-S adopted a cosine-like conformation that bridged CatK and tropocollagen, thereby stabilising the ternary complex. Unwinding occurred at the active site cleft, with Cys
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