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When it comes to blood clots, it is not only how they form that is crucial, but also how the body can break them down again. A team of researchers at the University of Koblenz, led by Prof. Dr Marie-T. Hopp, has demonstrated that haem – a component of haemoglobin – can influence this process. The findings provide a new molecular approach to better understanding the link between haemolysis and an increased risk of thrombosis.
How does the body break down blood clots?
Blood clots help to stop bleeding. To ensure that they do not subsequently block blood vessels permanently, they must be broken down. This process is known as fibrinolysis. During this process, the enzyme plasmin breaks down the stabilising protein network of the clot – known as fibrin – thereby enabling it to dissolve.
Haem inhibits the breakdown of blood clots
In certain diseases, red blood cells are destroyed at an increased rate. This process is known as haemolysis. During this process, labile haem can be released into the blood – an iron-containing component of haemoglobin that can interact with other proteins and influence their function.
Four female researchers at the University of Koblenz have now discovered that plasmin also binds haem with high affinity.
“We were able to demonstrate for the first time that plasmin binds haem with high affinity. Building on this, we investigated the effects of this strong interaction on fibrinolysis, that is, the natural breakdown of blood clots. Our findings now provide a new molecular insight that helps us better understand why people with certain haemolytic disorders face an increased risk of thrombosis,” explains Prof. Dr Marie-T. Hopp, head of the Bioorganic Chemistry research group at the University of Koblenz.
Using biochemical and biophysical methods, Hopp and her team investigated the binding of haem to plasmin. Their findings showed that plasmin can bind several haem molecules very rapidly. By analysing short peptides derived from plasmin and conducting supplementary computer simulations, the researchers identified six potential haem-binding sites. Three of the binding sites on the enzyme’s surface appeared particularly promising. The scientists also discovered that bound haem significantly inhibits plasmin’s ability to break down blood clots, with the extent of inhibition depending on the haem concentration. This effect was already observed at haem concentrations such as those that can occur in cases of pathologically increased destruction of red blood cells.
A potential building block for understanding the risk of thrombosis
The findings provide new insights into how excess haem impairs the body’s natural process of breaking down blood clots. Reduced fibrinolysis could contribute to the increased risk of thrombosis observed in certain haemolytic disorders. Further research is needed to determine whether, and to what extent, the haem-plasmin interaction actually plays a role in this process.
The results of the study were published on 21 October 2026 in the *International Journal of Biological Macromolecules*, a renowned international journal.
Prof. Dr. Marie-T. Hopp, University of Koblenz
Isabeau Weyand, Leonie A. Arenz, Lipi Raghunatha Reddy, Marie-T. Hopp: Attenuation of fibrinolysis through haem binding to the serine protease plasmin.
https://doi.org/10.1016/j.ijbiomac.2026.154990
A molecular view of the risk of thrombosis. Red blood cells in the blood (left) release haem during ...
Source: Marie-T. Hopp
Copyright: Marie-T. Hopp / University of Koblenz
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A molecular view of the risk of thrombosis. Red blood cells in the blood (left) release haem during ...
Source: Marie-T. Hopp
Copyright: Marie-T. Hopp / University of Koblenz
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