Interactions of endogenous ligands with human serum albumin
https://doi.org/10.29235/1561-8323-2026-70-2-141-152
Abstract
In this article we have analyzed the possibility of endogenous ligands (thyroxine, fatty acids, heme) displacing bilirubin from its binding site in the first domain of the human serum albumin based on in silico experiments. The obtained data showed that the known binding site in the first domain of human serum albumin is not specific for bilirubin. Indeed, the inhibition constant of the albumin and bilirubin complex was 417.38 µM, of the albumin and palmitic acid complex was 164.28 µM, of the albumin and heme complex was 10.13 µM, and of the albumin and thyroxine complex was 9.17 µM. The binding of fatty acids by human serum albumin should lead to changes in the tertiary structure of the protein and the appearance of more specific binding sites for 4Z,15Z-Bilirubin IXα.
About the Authors
V. A. Poboinev
Belarusian State Medical University
Belarus
Belarus
Poboinev Victor V. – Ph. D. (Biology), Associate Professor, Deputy Dean
83, Dzerzhynsky Ave., 220083, Minsk
A. N. Stojarov
Belarusian State Medical University
Belarus
Belarus
Stojarov Aleksander N. – D. Sc. (Biology), Professor, Professor of the Department
83, Dzerzhynsky Ave., 220083, Minsk
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