zhpsЖурнал прикладной спектроскопииZhurnal Prikladnoii Spektroskopii0514-7506B. I. Stepanov Institute of Physics of the National Academy of Scienceszhps-950Research ArticleСтатьиМежмолекулярные взаимодействия саксаглиптина и вилдаглиптина с сывороточным альбумином человекаIntermolecular interactions of saxagliptin and vildagliptin with human serum albuminBarghashS.BarghashS.

Каир

Analytical Chemistry Department, Faculty of Pharmacy (Girls), 

Cairo

Abd El-RazeqS.Abd El-RazeqS.

Каир

Analytical Chemistry Department, Faculty of Pharmacy (Girls), 

Cairo

ElmansiH.ElmansiH.

Мансура, 35516

Faculty of Pharmacy, 

Mansoura

dr_heba85@hotmail.comElmorsyM. A.ElmorsyM. A.

Мансура, 35516

Faculty of Pharmacy, 

Mansoura

BelalF.BelalF.

Мансура, 35516

Faculty of Pharmacy, 

Mansoura

Университет Аль-АзхарAl-Azhar UniversityУниверситет Аль-Азхар, КаирAl-Azhar UniversityУниверситет МансурыMansoura University202129112021886974974Copyright © Barghash S., Abd El-Razeq S., Elmansi H., Elmorsy M.A., Belal F., 20212021Barghash S., Abd El-Razeq S., Elmansi H., Elmorsy M.A., Belal F.Barghash S., Abd El-Razeq S., Elmansi H., Elmorsy M.A., Belal F.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://zhps.ejournal.by/jour/article/view/950

Изучены связывающие взаимодействия между сывороточным альбумином человека (HSA) и двумя антидиабетическими препаратами — саксаглиптином (SXG) и вилдаглиптином (VDG). Использованы различные подходы, включая естественную флуоресценцию, синхронную флуоресценцию, спектроскопию поглощения УФ-видимого диапазона, ИК-Фурье-спектроскопию (FTIR), в дополнение к моделированию стыковки молекул. При разных температурах определены термодинамические параметры взаимодействий. Показано, что собственная флуоресценция HSA подавляется по статическому механизму. Получены константы связывания Ka = 4.0×104, 2.49×104 и 2.42×104 л/моль для SXG и 1.13×104 , 8.54×103 и 7.15×103 л/моль для VDG при 298, 310 и 318 К соответственно. Данные сравнительного эксперимента с индикаторами места связывания показывают, что SXG и VDG связывают HSA в основном в положении I белка или рядом с ним. Согласно результатам FTIRспектроскопии, конформация белка изменяется в присутствии SXG или VDG. Результаты спектроскопического анализа свидетельствуют о том, что заметные изменения в конформации структуры белка происходят после добавления SXG или VDG. 

The binding interactions between human serum albumin (HSA) and two anti-diabetic drugs, saxagliptin (SXG) and vildagliptin (VDG), are studied. Different approaches are adopted, including native fluorescence, synchronous fluorescence, UV–Visible absorption, and Fourier-transform infrared (FTIR) analysis, in addition to molecular docking simulations. Moreover, the thermodynamic parameters of the interactions are determined at different temperatures. The obtained results indicate that the intrinsic fluorescence of HSA is quenched via a static mechanism. Values for the binding constant, Ka, are 4.0×104, 2.49×104, and 2.42×104 L/mol for SXG, and 1.13×104, 8.54×103, and 7.15×103 L/mol for VDG at 298, 310, and 318 K, respectively. Evidence from competition experiments with site markers indicate that both SXG and VDG bind HSA primarily at or near site I of the protein. FTIR spectroscopy data indicate an alteration of the protein conformation in the presence of SXG or VDG. Indeed, the results of different spectroscopic analyses indicated that noticeable changes in the protein structure conformation occur following the addition of SXG or VDG. 

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