This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Scientists have redefined how the key blood-clotting protein fibrinogen behaves when it contacts air, overturning two decades of scientific consensus on wound healing. It is the culmination of more than a decade of international collaboration by Dr.
Richard Campbell of The University of Manchester, Professor Juan Ruso of the University of Santiago de Compostela in Spain and Dr. Natalia Hassan of the Metropolitan Technological University in Chile. The discovery could have far-reaching implications for treating clotting disorders like hemophilia or providing health care for patients taking blood thinners like warfarin, as scabs that form on the surface of blood are vital to sealing wounds and keeping sites free of infection.
It could also explain aspects of how a lung can collapse in acute respiratory distress syndrome (ARDS), as fibrinogen disrupts the oily layer that keeps the airways open during breathing. It may also transform the design of biosensors that allow people to monitor how their blood is performing, as the sensors rely on understanding how proteins disrupt those surfaces. For more than 20 years, the field has relied on a "single tilting layer" model for fibrinogen, in which the long protein molecules lie flat on the surface at first and then lean upright as more arrive.
But the new study, published in the Journal of the American Chemical Society, shows the benchmark model missed that fibrinogen remains flat and builds multiple layers that stack like sheets of paper. These layers grow thicker and more complete as more molecules arrive. This new information helps explain how the long protein molecules line up on the surface of blood, where fibers called fibrin form the basis of the scab, a solid film formed during evaporation of fluid at the blood surface that seals a wound.
The scientists used an advanced technique called neutron reflectometry at the Institut Laue-Langevin (ILL) in France, where Campbell was formerly based. The team demonstrated that this behavior holds true across a wide range of concentrations and in very different solution conditions, showing the mechanism is not a rare quirk but a universal feature of fibrinogen when it contacts air. Principal investigator Campbell explained, "It's never easy challenging an established model of how molecules behave in nature.
"But by using the advanced technique of neutron reflectometry on the FIGARO instrument at the ILL research facility, we could see the structure of these protein surfaces in more detail than scientists had seen before. "Although lab data recorded in the past were compatible with the concept of a 'single tilting layer' model, our new data show multiple layering as a fundamentally different way of working." Dr. Glenn Coope, a former Ph.D. student at The University of Manchester who is now based at Lund University in Sweden, said, "When the COVID-19 pandemic struck, I spent time analyzing structural data on how fibrinogen gathered at liquid surfaces while working from home.
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