Scientists have discovered that blood clots form in a fundamentally different way from previously understood, with significant implications for wound care and clotting disorder treatments. An international research team at the Institut Laue-Langevin (ILL) in France used neutron reflectometry to study how fibrinogen, a cylindrical blood protein, forms a surface layer when exposed to air. Contrary to the long-held belief that fibrinogen molecules accumulate in a single upward-tilted layer, the ILL experiments revealed that the protein remains flat and stacks in multiple layers like sheets of paper. "It's never easy challenging an established model of how molecules behave in nature," said Richard Campbell, the project leader from the University of Manchester.

The findings, published in the Journal of the American Chemical Society, may improve treatments for patients with blood-clotting disorders such as haemophilia or those on blood-thinning medications. They could also enhance glucose monitoring devices for diabetics and treatment of acute respiratory distress syndrome (ARDS), where fibrinogen leakage from blood vessels causes fatal oxygen absorption issues. Glenn Coope from Lund University began studying fibrinogen structural data during the pandemic, noting the findings may help understand ARDS behavior. Robert Jacobs from Oxford University highlighted that further experiments are needed to determine the significance of this multilayer organization in complex biological environments.