Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54379 МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ INTERACTION OF CHAPERONE Skp FROM YERSINIA PSEUDOTUBERCULOSIS WITH MULTIDOMAIN PROTEINS AT THE DIFFERENT pH VALUES OF MEDIUM ВЗАИМОДЕЙСТВИЕ ШАПЕРОНА Skp ИЗ Yersiniapseudotuberculosis С МУЛЬТИДОМЕННЫМИ БЕЛКАМИ ПРИ РАЗНЫХ ЗНАЧЕНИЯХ pH СРЕДЫ Сидорин Е В Sidorin E V sev1972@mail.ru Хоменко В. А. Khomenko V. A. Соловьева Т. Ф. Soloveva T. F. Тихоокеанский институт биоорганической химии им. Г.Б. Елякова ДВО РАН ru G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences ru Тихоокеанский институт биоорганической химии им. Г.Б. Елякова ДВО РАН Владивосток Россия G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences Vladivostok Russian Federation Тихоокеанский институт биоорганической химии им. Г.Б. Елякова ДВО РАН Владивосток Россия G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences Vladivostok Russian Federation 25 12 2018 25 12 2018 3 4 869 873 20 12 2018 20 12 2018 https://rusjbpc.ru/en/nauka/article/54379/view

Белок Skp Yersinia pseudotuberculosis выполняет функции периплазматического шаперона в бактериях и обладает способностью связывать IgG человека и кролика. Данная работа посвящена изучению влияния этого шаперона на агрегацию IgG человека при разных значениях pH среды. Для решения этой задачи с помощью метода динамического рассеяния света была исследована кинетика агрегации rSkp, IgG и IgG в присутствии шаперона в кислом, нейтральном и щелочном растворах. Было показано, что в присутствии rSkp скорость процессов самоассоциации и агрегации IgG существенно снижается. Полученные результаты демонстрируют рН-зависимый характер шаперонной и иммуноглобулинсвязывающей активности rSkp. Наиболее устойчивые низкомолекулярные комплексы (RH до 10 нм) между шапероном и IgG человека образуются при кислых значениях рН среды. В случае защелачивания реакционной среды шаперонная активность rSkp снижается, и агрегация IgG хотя и замедляется, но в меньшей степени, чем при кислом рН. Полученная информация может представлять интерес для разработчиков стабильных и качественных биофармацевтических препаратов на основе иммуноглобулинов.

Protein Skp Yersinia pseudotuberculosis serves as the periplasmic chaperone in bacteria and has the ability to bind human and rabbit IgG. This work is aimed at studying the effect of this chaperone on the aggregation of human IgG at various pH values of the medium. To solve this problem, the aggregation kinetics of rSkp, IgG, and IgG in the presence of a chaperone in acidic, near neutral, and basic solutions was studied using the dynamic light scattering method. It was shown that in the presence of rSkp, the rate of IgG self-association and aggregation decreases significantly. The obtained results demonstrate the pH-dependent character of the chaperone and immunoglobulin-binding activities of rSkp. The most stable low-molecular complexes (RH up to 10 nm) between chaperone and human IgG are formed at acidic pH values of the medium. In the case of alkalinization of the reaction medium, the chaperone activity of rSkp decreases, and the aggregation of IgG although slows, but to a lesser extent than at acidic pH. The information obtained may be of interest to developers of stable and high-quality biopharmaceuticals based on immunoglobulins.

 шаперон Skp Yersinia pseudotuberculosis агрегация белков белок-белковые взаимодействия динамическое рассеяние света chaperone Skp Yersinia pseudotuberculosis aggregation of proteins protein-protein interactions dynamic light scattering

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