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While fibrin's fracture behavior under monotonic loading has been intensively explored, its fatigue mechanism that governs thrombus embolization is understudied. Multiscale experiments, modeling of condensed fibrin networks, reveal a paradoxically low fatigue threshold despite high fracture energy. Mechanistically, cyclic loading induces irreversible \u03b1\u2010to\u2010\u03b2 transitions in fibrin's molecular chains, causing molecular creep that dissipates strain energy, propagates cracks via rupture of stress\u2010localized fibers. A multiscale continuum model quantitatively links this nanoscale mechanics to macroscale fatigue, providing an alternative mechanism of thrombus rupture as a molecular disorder driven by cumulative conformational damage. These findings reexamine widely adopted fibrous hydrogel design paradigms while bridging molecular structure characteristics to clinical thrombosis\u2013a critical step toward predictive rupture risk assessment, targeted therapeutic strategies.<\/jats:p>","DOI":"10.1002\/advs.202505109","type":"journal-article","created":{"date-parts":[[2025,8,8]],"date-time":"2025-08-08T06:14:06Z","timestamp":1754633646000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Molecular Creep Induced Fatigue Rupture of Fibrin Clots"],"prefix":"10.1002","volume":"12","author":[{"given":"Dani","family":"Liu","sequence":"first","affiliation":[{"name":"Institute of Solid Mechanics School of Aeronautic Science and Engineering Beihang University  Beijing 100191 China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zichang","family":"Jia","sequence":"additional","affiliation":[{"name":"Department of Interventional Radiology, 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