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Current antiplatelet drugs are designed either to indirectly inhibit intracellular signaling pathways that activate integrin \u03b1IIb\u03b23 or to directly block the binding of the activated integrin to fibrinogen. However, because this interaction is also essential for normal hemostasis, these drugs inevitably increase the risk of serious spontaneous bleeding. In this study, we aimed to develop a safer strategy to prevent thrombosis without impairing hemostasis. Building on our previous findings that the transmembrane domain (TMD) of integrin \u03b23 undergoes distinct topological changes during force\u2010 vs. agonist\u2010dependent activation, we targeted the \u03b2\u2010tail domain of integrin \u03b23 as an epitope for an antibody that selectively blocks force\u2010induced changes. This antibody specifically inhibits force\u2010dependent \u03b1IIb\u03b23 activation, a key driver of platelet aggregation at atherosclerotic lesions, and suppresses platelet aggregation in ex vivo and in vivo models without inducing bleeding. From these results, we conclude that this approach offers a promising therapeutic strategy to prevent thrombosis while minimizing bleeding risk, addressing a major limitation of current antiplatelet therapy.<\/jats:p>","DOI":"10.1002\/advs.202522086","type":"journal-article","created":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T11:59:11Z","timestamp":1776081551000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Selective Inhibition of Integrin \u03b23 Topology Provides a Safer Antithrombotic Strategy"],"prefix":"10.1002","volume":"13","author":[{"given":"Joonha","family":"Lee","sequence":"first","affiliation":[{"name":"Department of Life Sciences Korea University  Seoul Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chul\u2010Gyun","family":"Lim","sequence":"additional","affiliation":[{"name":"Department of Life Sciences Korea University  Seoul Republic of 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