Portrait of "good" cholesterol
The molecular structure of "good cholesterol" has been determined
ChemPort based on materials from the University of Cincinnati:
'Good Cholesterol' Structure Identified, Could Explain Protective EffectsResearchers from the group of Sean Davidson (W. Sean Davidson) from the University of Cincinnati have determined the structure of cholesterol-containing high-density lipoproteins in humans.
They claim that the results of their study can explain how "good cholesterol" protects against cardiovascular diseases, including heart attacks and strokes.
High-density lipoproteins (HDL) also known as "good cholesterol" are molecular complexes of fats and proteins that deliver fats to certain fragments in the human body. Recently, significant efforts have been made to create drugs that increase the level of HDL, while working in parallel with drugs that lower the content of "bad cholesterol" or low-density lipoproteins (LDL). The study of synthetic HDLs has shown that with a certain protein-lipid ratio, lipoproteins can acquire anti-inflammatory or antioxidant properties.
The structure of the protein part of high-density lipoproteins –
the so-called "good cholesterol".
Figure from the article by Rong Huang et al.
Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma
Nature Structural & Molecular Biology (2011)
Davidson notes that at the moment little is known about what causes the protective properties of HDL at the molecular level. The lack of such information is primarily due to the fact that the structure of HDL has not been accurately established to date. Researchers from Davidston's group were able to isolate human HDL and study its three-dimensional structure in the conformation in which HDLs move through human plasma.
According to Davidson, previous studies were aimed at studying the structure of only synthetic HDL, while the isolation of human HDL allowed us to focus on the study of natural high-density lipoproteins. The researchers studied the isolated HDLs using mass spectrometry and other methods, finding that HDL proteins form a cell in which fats are encapsulated. Most of the HDL particles circulating in human blood plasma have the same structure, but the protein shell can change its shape, adjusting to the structure and size of the fat molecule.
The study of the structure of human HDL allowed us to conclude that most of the interactions that determine the physiological properties of "good cholesterol" are caused by an ensemble of interactions of the protein apolipoprotein A-I (apolipoprotein A-I) – a protein located on the surface of the HDL particle.
Portal "Eternal youth" http://vechnayamolodost.ru16.03.2011