pmedpharmФармация и фармакологияPharmacy & Pharmacology2307-92662413-2241Pyatigorsk Medical and Pharmaceutical Institute - branch of Volgograd State Medical Univer10.19163/2307-9266-2021-9-4-306-317pmedpharm-884Research ArticleФАРМАКОЛОГИЯ И КЛИНИЧЕСКАЯ ФАРМАКОЛОГИЯPHARMACOLOGY AND CLINICAL PHARMACOLOGYВЛИЯНИЕ НЕКОТОРЫХ D-МЕТАЛЛОВ НА ОБРАЗОВАНИЕ КОНЕЧНЫХ ПРОДУКТОВ ГЛИКИРОВАНИЯ, АГРЕГАЦИЮ И АМИЛОИДНУЮ ТРАНСФОРМАЦИЮ АЛЬБУМИНА В РЕАКЦИИ ГЛИКИРОВАНИЯINFLUENCE OF CERTAIN D-METALS ON FORMATION OF ADVANCED GLYCATION END PRODUCTS, AGGREGATION AND AMYLOID TRANSFORMATION OF ALBUMIN IN GLYCATION REACTIONhttps://orcid.org/0000-0002-0162-0653ЛитвиновР. А.LitvinovR. A.

кандидат медицинских наук, старший научный сотрудник лаборатории метаботропных лекарственных средств отдела фармакологии и биоинформатики Научного центра инновационных лекарственных средств с опытно-промышленным производством Волгоградского государственного медицинского университета; научный сотрудник лаборатории экспериментальной фармакологии ГБУ «Волгоградский медицинский научный центр»

Candidate of Sciences (Medicine), Senior Researcher, Laboratory of Metabotropic Medicines, Department of Pharmacology and Bioinformatics, Scientific Center for Innovative Medicines with Pilot Production, Volgograd State Medical University; Researcher, Laboratory of Experimental Pharmacology, Volgograd Medical Research Center

litvinov.volggmu@mail.ruГонтареваА. В.GontarevaA. V.

студент 6-го курса, специальность «Медицинская биохимия», ФГБОУ ВО «Волгоградский государственный медицинский университет» Минздрава России, соисполнитель гранта Президента Российской Федерации для поддержки молодых ученых, кандидатов наук МК-1887.2020.7

6th year student, specialty “Medical Biochemistry”, Volgograd State Medical University, co-executor of the grant of the President of the Russian Federation to support young scientists, candidates of sciences MK-1887.2020.7

arinaarinag@gmail.comУсмияноваЛ. Э.UsmiyanovaL. E.

студент 6-го курса, специальность «Медицинская биохимия», ФГБОУ ВО «Волгоградский государственный медицинский университет» Минздрава России, соисполнитель гранта Президента Российской Федерации для поддержки молодых ученых, кандидатов наук МК-1887.2020.7

6th year student, specialty “Medical Biochemistry”, Volgograd State Medical University, co-executor of the grant of the President of the Russian Federation to support young scientists, candidates of sciences MK-1887.2020.7

mila.getmanets@gmail.comКлименкоД. Р.KlimenkoD. R.

студентка 4-го курса, специальность «Фармация», ФГБОУ ВО «Волгоградский государственный медицинский университет» Минздрава России

4th year student, specialty “Pharmacy”, Volgograd State Medical University

vip.klimenko.darya@mail.ru1. Федеральное государственное бюджетное образовательное учреждение высшего образования «Волгоградский государственный медицинский университет» Министерства здравоохранения Российской Федерации 400131, Россия, г. Волгоград, площадь Павших Борцов, д. 1 2. Государственное бюджетное учреждение «Волгоградский медицинский научный центр» 400131, Россия, г. Волгоград, площадь Павших Борцов, д. 1Россия1. Volgograd State Medical University 1, Pavshikh Bortsov Sq., Volgograd, Russia, 400131 2. Volgograd Medical Research Center, 1, Pavshikh Bortsov Sq., Volgograd, Russia, 400131Russian FederationФедеральное государственное бюджетное образовательное учреждение высшего образования «Волгоградский государственный медицинский университет» Министерства здравоохранения Российской Федерации 400131, Россия, г. Волгоград, площадь Павших Борцов, д. 1РоссияVolgograd State Medical University 1, Pavshikh Bortsov Sq., Volgograd, Russia, 400131Russian Federation20210809202194306317Copyright © Литвинов Р.А., Гонтарева А.В., Усмиянова Л.Э., Клименко Д.Р., 20212021Литвинов Р.А., Гонтарева А.В., Усмиянова Л.Э., Клименко Д.Р.Litvinov R.A., Gontareva A.V., Usmiyanova L.E., Klimenko D.R.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.pharmpharm.ru/jour/article/view/884Цель

Цель. Исследование влияния фактора протекания реакции гликирования бычьего сывороточного альбумина (БСА) глюкозой и фактора присутствия в среде реакции гликирования катионов d-металлов (никель (II), кобальт (II), железо (II), железо (III), медь (II) или цинк (II)) на процесс агрегации и амилоидной трансформации БСА. Установление влияния указанных катионов на интенсивность образования конечных продуктов реакции гликирования (КПГ) и интенсивность флуоресценции аминокислот тирозин и триптофан.

Материалы и методы

Материалы и методы. Реагенты в реакции гликирования: глюкоза (в конечной концентрации 0,36 М), БСА (в конечной концентрации 1 мг/мл), деионизированная вода, один из катионов d-металлов, а именно никель (II), кобальт (II), железо (II), железо (III), медь (II) или цинк (II) (в виде соли хлорида, сульфата или нитрата, в конечной концентрации 40 мкМ). Условия протекания реакции гликирования: инкубация 24 ч при температуре 60°С. Исследовано влияние двух факторов (фактор протекания гликирования и фактор присутствия иона d-металла в реакционной среде) на концентрацию КПГ, образуемых в ходе реакции гликирования, на интенсивность флуоресценции аминокислот триптофан и тирозин, на агрегацию БСА и на способность БСА к амилоидной трансформации в описанных условиях.

Результаты

Результаты. Установлено, что исследуемые факторы статистически значимо влияют на рассматриваемые параметры. Наивысшая активность установлена для иона меди (II), который интенсифицирует образование КПГ в пробах, где протекает гликирование, снижает интенсивность флуоресценции аминокислот триптофан и тирозин (самостоятельно и усиливая эффект на фоне гликирования), вызывает агрегацию БСА (самостоятельно и усиливая эффект на фоне гликирования), вызывает амилоидную трансформацию БСА (самостоятельно и усиливая эффект на фоне гликирования). Наименее выражены перечисленные эффекты были в реакционных средах с добавлением никеля (II) или кобальта (II). Данные катионы снижают интенсивность образования КПГ, не вызывают образования белковых агрегатов. В присутствии глюкозы никель (II) слабо подавляет интенсивность флуоресценции триптофана и тирозина, незначительно усиливает амилоидную трансформацию БСА. Кобальт (II) незначительно подавляет амилоидную трансформацию БСА. Катионы железа (II), железа (III) и цинка (II) по выраженности и характеру эффектов занимают промежуточное положение между медью (II) с одной стороны, и никелем (II) и кобальтом (II) с другой стороны, в разной степени сочетая влияние на образование КПГ, интенсивность флуоресценции триптофана и тирозина, агрегацию и амилоидную трансформацию БСА. В отсутствии глюкозы способность цинка (II) вызывать образование белковых агрегатов оказалась наивысшей, а его способность стимулировать амилоидную трансформацию БСА соответствовала таковой у меди (II).

Заключение

Заключение. Присутствие катионов d-металлов влияет на интенсивность образования КПГ в реакции гликирования, влияет на интенсивность амилоидной трансформации БСА и на образование агрегатов белка. В ряду таких ионов, как никель (II), кобальт (II), железо (II), железо (III), медь (II) и цинк (II), ионы меди (II) оказались наиболее активными по способности ускорять образование КПГ, подавлять флуоресценцию триптофана и тирозина, усиливать агрегацию и амилоидную трансформацию БСА в реакции гликирования. Наименьшая выраженность указанных свойств отмечается для ионов никеля (II) и кобальта (II)

The aim of the research is to investigate the influence of the factor of the glycation behavior of bovine serum albumin (BSA) by glucose, and the factor of d-metal cations (nickel (II), cobalt (II), iron (II), iron (III), copper (II) or zinc (II)) presence, on the process of aggregation and the amyloid transformation of BSA and, therefore, to establish the effect of these cations on the rate of the formation of advanced glycation end products (AGEs), and the intensity of fluorescence of the amino acids tyrosine and tryptophan.

Materials and methods

Materials and methods. Reagents in the glycation are: glucose (at the final concentration of 0.36 M), BSA (at the final concentration of 1 mg/ml), deionized water, one of the d-metal cations, i. e. nickel (II), cobalt (II), iron (II), iron (III), copper (II) or zinc (II) (in the form of chloride, sulfate or nitrate salts, at the final concentration of 40 μM). The conditions for the glycation reaction are the incubation for 24 hours at the temperature of 60°C. The influence of two factors (the factor of the glycation reaction and the factor of a d-metal ion presence in the reaction medium) on the concentration of glycation end products (AGEs) formed during the glycation reaction, on the fluorescence intensity of the amino acids tryptophan and tyrosine, on the aggregation of BSA, and on the ability of BSA to the amyloid transformation under the described conditions, have been studied.

Results

Results. It was found out that the studied factors have a statistically significant effect on the considered parameters. The highest activity was found for the copper ion (II), which intensifies the formation of the AGEs in the samples where glycation occurs, reduces the fluorescence intensity of the amino acids’ tryptophan and tyrosine (independently and increasing the effect against the background of glycation). Besides, it independently causes the aggregation of BSA hereby intensifying the effect against the background of glycation, it independently causes the amyloid transformation of BSA enhancing the effect against the background of glycation. The above-listed effects were the least pronounced in the reaction media with the addition of nickel (II) or cobalt (II). These cations reduce the rate of the AGEs formation, do not cause the formation of protein aggregates. In the presence of glucose, nickel (II) weakly suppresses the fluorescence intensity of tryptophan and tyrosine, and slightly enhances the amyloid transformation of BSA. Cobalt (II) slightly inhibits the amyloid transformation of BSA. In terms of the severity and nature of the effects, the iron (II), iron (III) and zinc (II) cations occupy an intermediate position between copper (II), on the one hand, and nickel (II) and cobalt (II), on the other hand, combining the influence on the AGEs formation, the intensity of fluorescence of tryptophan and tyrosine, the aggregation and amyloid transformation of BSA. In the absence of glucose, the ability of zinc (II) to induce the formation of protein aggregates turned out to be the highest, and its ability to stimulate the amyloid transformation of BSA corresponded to that of copper (II).

Conclusion

Conclusion. The presence of d-metal cations affects the rate of the AGEs formation in the glycation reaction, affects the rate of the BSA amyloid transformation and the protein aggregates formation. Among such ions as nickel (II), cobalt (II), iron (II), iron (III), copper (II) and zinc (II), copper (II) ions turned out to be the most active in their ability to accelerate the AGEs formation, suppress the fluorescence of tryptophan and tyrosine, enhance the aggregation and amyloid transformation of BSA in the glycation reaction. The least manifestation of these properties is observed for nickel (II) and cobalt (II) ions.

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