danДоклады Национальной академии наук БеларусиDoklady of the National Academy of Sciences of Belarus1561-83232524-2431The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"10.29235/1561-8323-2026-70-2-141-152dan-1304Research ArticleБИОЛОГИЯBIOLOGYВзаимодействия эндогенных лигандов с сывороточным альбумином человекаInteractions of endogenous ligands with human serum albuminПобойневВ. В.PoboinevV. A.

Побойнев Виктор Витольдович – канд. биол. наук,доцент, заместитель декана

пр. Дзержинского, 83, 220083, Минск

Poboinev Victor V. – Ph. D. (Biology), Associate Professor, Deputy Dean

83, Dzerzhynsky Ave., 220083, Minsk

dremozzew@mail.ruСтожаровА. Н.StojarovA. N.

Стожаров Александр Николаевич – д-р биол. наук,профессор, профессор кафедры

пр. Дзержинского, 83, 220083, Минск

Stojarov Aleksander N. – D. Sc. (Biology), Professor, Professor of the Department

83, Dzerzhynsky Ave., 220083, Minsk

stojarov@mail.ruБелорусский государственный медицинский университетBelarusian State Medical University202604052026702141152Copyright © Побойнев В.В., Стожаров А.Н., 20262026Побойнев В.В., Стожаров А.Н.Poboinev V.A., Stojarov A.N.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://doklady.belnauka.by/jour/article/view/1304

На основании in silico экспериментов проанализирована возможность эндогенных лигандов (тироксина, жирных кислот, гема) вытеснять билирубин из его сайта связывания в первом домене сывороточного альбумина человека. По результатам проведенных исследований показано, что сайт связывания в первом домене сывороточного альбумина не является специфическим для билирубина. Константа ингибирования комплекса альбумина и билирубина составила 417,38 мкмоль/л, комплекса альбумина и пальмитиновой кислоты – 164,28 мкмоль/л, комплекса альбумина и гема – 10,13 мкмоль/л, комплекса альбумина и тироксина – 9,17 мкмоль/л. Сделан вывод, что связывание жирных кислот сывороточным альбумином человека должно приводить к изменению пространственной структуры белка и появлению на нем более специфичных сайтов связывания для физиологического изомера билирубина.

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. 

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The authors declare that there are no conflicts of interest present.