A Mathematical Model of Bivalent Binding Suggests Physical Trapping of Thrombin within Fibrin Fibers.

ABSTRACT: Thrombin is an enzyme that plays many important roles in the blood clotting process; it activates platelets, cleaves coagulation proteins within feedback loops, and cleaves fibrinogen into fibrin, which polymerizes into fibers to form a stabilizing gel matrix in and around growing clots. Thrombin also binds to the formed fibrin matrix, but this interaction is not well understood. Thrombin-fibrin binding is often described as two independent, single-step binding events, one high-affinity and one low-affinity. However, kinetic schemes describing these single-step binding events do not explain experimentally-observed residency times of fibrin-bound thrombin. In this work, we study a bivalent, sequential-step binding scheme as an alternative to the high-affinity event and, in addition to the l

SUBMITTER: Kelley M 

PROVIDER: S-EPMC6817721 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature