Molecular docking shows potential inhibition of HMG-CoA reductase in hypercholesterolemia, suggesting new therapeutic options.
Hypercholesterolemia is one of the major risk factors of cardiovascular diseases. HMG-CoA reductase enzyme, the main drug target to reduce the cholesterol levels, catalyzes biosynthesis of cholesterol. In addition to in-silico estimations of ADMET profiles of compounds composed of several functional groups which are known to be effective for many diseases, a molecular docking study was performed to investigate binding modes of compounds in binding site of HMG-CoA reductase. Prior to docking studies, the RESP charges of compounds were defined by quantum mechanics calculations. Analyzes revealed that eleven Schiff base derivatives showed better binding rather than co-crystalized drug Rosuvastatin. Results demonstrated that Schiff base group included compounds have better inhibition effects on HMG-CoA reductase than their related pre-compounds. The docking scores of compounds range between -7.22 kcal/mol and -9.43 kcal/mol. The compounds L16, L28, and L15 were the ligands having best binding scores with the values -9.43 kcal/mol, -9.24 kcal/mol, and -9.23 kcal/mol, respectively. The analyses showed that compounds interact with several key residues of enzyme such as Glu559, Asp690, Lys691, Lys692, and Asp767.
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Selami Ercan (2025) studied this question.
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