Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54426 МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ SPECTRAL AND LUMINESCENCE CHARACTERISTICS OF THE AMYLOID STRUCTURES COMPLEXES WITH BLOOD PROTEINS СПЕКТРАЛЬНО-ЛЮМИНЕСЦЕНТНЫЕ ХАРАКТЕРИСТИКИ КОМПЛЕКСОВ АМИЛОИДНЫХ СТРУКТУР С БЕЛКАМИ КРОВИ Гармаза Ю М Harmaza Y M garmaza@yandex.ru Зубрицкая Г П Zubritskaya H P Слобожанина Е И Slobozhanina E I ГНУ «Институт биофизики и клеточной инженерии НАН Беларуси» ru Institute of Biophysics and Cell Engineering of National Academy of Sciences of Belarus ru ГНУ «Институт биофизики и клеточной инженерии НАН Беларуси» ru Institute of Biophysics and Cell Engineering of National Academy of Sciences of Belarus ru ГНУ «Институт биофизики и клеточной инженерии НАН Беларуси» ru Institute of Biophysics and Cell Engineering of National Academy of Sciences of Belarus ru 25 06 2019 25 06 2019 4 2 237 244 20 06 2019 20 06 2019 https://rusjbpc.ru/en/nauka/article/54426/view

Анализ параметров флуоресценции тиофлавина Т, который является специфичным для обнаружения амилоидных фибрилл, и параметров собственной флуоресценции белков крови позволил установить, что образование комплекса “амилоидные структуры - белки плазмы крови” зависит от температуры инкубации, так как связи между белками и их лигандами ослабевают при повышенных температурах. Продемонстрировано, что изменение рН среды инкубации, как в кислую, так и в щелочную области также сказывается на образовании комплексов сывороточного альбумина с амилоидными структурами, по-видимому, в результате изменения связывающей способности альбуминов при их окислении. Выявлено, что эссенциальные (Zn, Cu) микроэлементы, взаимодействуя с комплексом “амилоидные структуры - белки плазмы крови”, приводят к модификации параметров собственной и зондовой флуоресценции, что подтверждает предположение о существовании металл-связывающих сайтов в амилоидных фибриллах для ионов металлов.

Analysis of the fluorescence parameters of thioflavin T, which is specific for the amyloid fibrils detection, and the parameters of the intrinsic fluorescence of blood proteins allowed to establish that the formation of the complex "amyloid structures - serum proteins" depends on the incubation temperature because of the bonds between proteins and their ligands become weaker under elevated temperatures. It was demonstrated that alteration of the incubation medium pH, both to the acidic and alkaline region, also affects on the formation of the complexes of serum albumin with amyloid structures, apparently as a result of the albumins binding ability changing during their oxidation. It was found that essential (Zn, Cu) trace elements interacting with the complex "amyloid structures - serum proteins" lead to modification of parameters as an intrinsic fluorescence as a fluorescent probe, that confirms the assumption about existence of the metal-binding sites in amyloid fibrils for metal ions.

 амилоидные структуры белки крови спектральные характеристики физико-химические факторы amyloid structures blood proteins spectral characteristics physical and chemical factors

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