How fibrin networks form a blood clot

Role of extended knob-hole interaction sites in fibrin polymerisation and clot stability (Mr Nathan Asquith)

Supervised by Professor Robert Ariens, a PhD student is investigating the intricate processes behind blood clotting – the process that prevents excessive bleeding after an injury. Blood clotting is a rapid process, during which a protein called fibrinogen converts into fibrin. Fibrin forms a network that functions as the backbone of the clot, providing mechanical strength. Researchers have recently identified some of the precise locations on fibrin that proteins interact with to form the network. But scientists believe there are more interaction sites, and identifying these could reveal new ways to prevent harmful blood clots. In this project, the researchers are deciphering exactly how fibrin molecules bind together to form the clot backbone. They are making proteins in the lab that have alterations in the interaction sites before studying how they behave when clots form. They hope to discover new fibrin interaction sites that can be targeted by drugs to prevent clotting. A better understanding of the molecular interactions that underpin blood clot formation will help reveal why and how blood clots occur and using this knowledge we can design drugs to prevent or treat them.