vestichИзвестия Национальной академии наук Беларуси. Серия химических наукProceedings of the National Academy of Sciences of Belarus, Chemical Series1561-83312524-2342The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"10.29235/1561-8331-2019-55-4-447-454vestich-488Research ArticleБИООРГАНИЧЕСКАЯ ХИМИЯBIOORGANIC CHEMISTRYКонструирование иммуноглобулинсвязыващих пептидов на основе анализа взаимодействия протеина A Staphylococcus aureus с Fc-фрагментом иммуноглобулиновConstruction of immunoglobulin-binding peptides based on analysis of the protein A of Staphylococcus aureus interaction with immunoglobulins Fc fragmentЛапкоА. В.LapkoA. V.

Лапко Анастасия Викторовна – научный сотрудник. 

ул. акад. В. Ф. Купревича, 5/2, 220141, Минск

Anastasiya V. Lapko – Researcher.

5/2, acad. V. F. Kuprevich Str., 220141, Minsk

gormoshkina@gmail.comПустюльгаЕ. С.Pustyul’gaE. S.

Пустюльга Егор Сергееевич – младший научный сотрудник. 

ул. акад. В. Ф. Купревича, 5/2, 220141, Минск

Egor S. Pustyul’ga – Junior Researcher.

5/2, acad. V. F. Kuprevich Str., 220141, Minsk

zeroed.inside@gmail.comГолубовичВ. П.GolubovichV. P.

Голубович Владимир Петрович – доктор биологических наук, профессор, зав. лабораторией.

ул. акад. В. Ф. Купревича, 5/2, 220141, Минск

Vladimir P. Golubovich – D. Sc. (Biology), Professor, Head of the Laboratory. 

5/2, acad. V. F. Kuprevich Str., 220141, Minsk

golubovich@iboch.byИнститут биоорганической химии Национальной академии наук БеларусиInstitute of Bioorganic Chemistry of the National Academy of Sciences of Belarus201906122019554447454Copyright © Лапко А.В., Пустюльга Е.С., Голубович В.П., 20192019Лапко А.В., Пустюльга Е.С., Голубович В.П.Lapko A.V., Pustyul’ga E.S., Golubovich V.P.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://vestichem.belnauka.by/jour/article/view/488

За последние десятилетия молекулярный докинг становится все более популярным инструментом в разработке новых препаратов. Для поиска и дизайна новых соединений необходимо детальное изучение взаимодействия уже существующих комплексов лигандов с белком-мишенью. С целью установления перечня аминокислотных остатков В-домена протеина А Staphylococcus aureus, которые образуют связи с иммуноглобулинами класса G, проводилось изучение механизмов взаимодействия при образовании комплекса протеина А клеточной стенки золотистого стафилококка и иммуноглобулинов класса G методом молекулярного докинга. По данным молекулярного докинга нами были отобраны четыре аминокислотных остатка Phe132, Gln129, Tyr133 и Phe124, на основании которых можно сконструировать пептидный аналог активного центра связывания протеина А с Fc-фрагментом иммуноглобулинов класса G. Полученные результаты могут послужить отправной точкой для эффективной стратегии поиска новых средств для медицины, в частности для дальнейшей разработки биоспецифического сорбента для избирательного удаления иммуноглобулинов класса G из крови человека.

Over the past decades, molecular docking has become an increasingly popular tool for the development of new drugs. To search and design new compounds, a detailed study of the interaction of existing complexes of ligands with the target protein is necessary. According to the purpose to identify amino acid residues of the B domain of protein A of Staphylococcus aureus involved in interaction with immunoglobulins G, we studied the interaction mechanisms during the formation of a complex of protein A of the Staphylococcus aureus cell wall and immunoglobulins G by molecular docking. By the means of molecular docking we selected four amino acid residues of Phe132, Gln129, Tyr133 and Phe124, which we can use to construct a peptide analog of the active binding site of protein A with the Fc fragment of immunoglobulins G. The obtained results can serve as starting point for an effective strategy for finding new medicines, in particular, they can be used to further develop biospecific sorbent for the selective removal of immunoglobulins G from human blood.

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