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Researchers from the University of Missouri have for the first time been able to study in detail the structure of the ApoB100 protein, which plays a key role in the formation of low-density lipoproteins known as “bad” cholesterol. The discovery, published in the journal Nature, could lead to the development of new treatments for cardiovascular disease and more accurate diagnostic tests.
Using advanced cryo-electron microscopy and artificial intelligence, scientists were able to obtain a three-dimensional image of the complex structure of ApoB100. This protein acts as a protective framework for low-density lipoprotein particles, helping them move through the bloodstream. A better understanding of its structure may allow the development of drugs that target “bad” cholesterol, reducing the risk of heart disease and minimizing the side effects of standard statins.
The researchers emphasize that cholesterol itself is not exceptionally harmful - it is involved in the production of hormones and maintaining the structure of cell membranes. However, an excess of low-density lipoproteins can lead to the formation of atherosclerotic plaques and an increased risk of heart attacks and strokes. The new data on the structure of ApoB100 opens up the possibility of creating more accurate diagnostic methods - for example, measuring the amount of this protein in the blood to assess cardiovascular disease risk.
The study is of particular importance to the scientists because both authors have a family history of cardiovascular disease. They hope that their work will not only help to understand the fundamental mechanisms of fat and cholesterol metabolism, but will also lead to more effective prevention and treatment methods that could save millions of lives.