Unravelling the web like structure of blood clots

Deciphering the role of fibrin intrafibrillar structure and protofibril arrangements in blood clot structure, function and stability

Professor Robert Ariens and his colleagues at the University of Leeds are studying how fibrin contributes to dangerous blood clots. Fibrin is a thread-like protein that forms a 3D network of fibres, which holds the blood clot together. Fibrin fibres have a remarkable ability to stretch without breaking. They can be stretched more than five times their original size, which is more than spider silk, making fibrin the most stretchable biological fibre known to man. Recently, scientists have discovered abnormal fibrin clot structures in people with life threatening blood clots (thrombosis). But breaking down fibrin with clot busting drugs is notoriously difficult and not always successful. One reason for this is that we don’t yet fully understand how fibrin molecules are packed together inside fibrin fibres. Professor Ariens believes the way fibrin molecules are arranged inside the fibre networks is responsible for the clot’s resistant to stretch and breakdown. In this project, he will use state-of-the-art methods to study the structure of blood clots and investigate how the fibre arrangements change the stretch of the fibres and their sensitivity to clot busting drugs. This research will provide a deeper understanding of the structure and mechanisms behind the fibrin clot and may help the design of new drugs that remove damaging clots and treat thrombosis.