Dezhampanah Hamid, Mohammadi Asadollah, Mousazadeh Moghaddam Pour Amineh
Department of Chemistry, Faculty of Science, University of Guilan, Rasht, Iran.
Laboratory of Chemistry, Caspian Tamin Pharmaceutical Co, Rasht, Iran.
J Biomol Struct Dyn. 2023 Feb;41(3):970-981. doi: 10.1080/07391102.2021.2015444. Epub 2021 Dec 15.
This research was performed using spectroscopic techniques and molecular docking to elucidate the mechanisms of interaction between bovine serum albumin (BSA) and two novel synthesized azo dyes. The titration of dyes into BSA solution results in quenching of fluorescence emission by complex formation. The UV-Vis spectroscopy confirms that formation of complex in ground state between both dyes and BSA induces conformational and micro environmental changes of the protein. Based on the calculation of the thermodynamic parameters, it can be concluded that both dyes spontaneously bind onto BSA, and van der Waals force and hydrogen bonding interaction played a predominant roles in the process of spontaneous bonding. The average binding distance (r) between protein and both dyes was calculated by Förster energy transfer measurements and revealed both dyes bind to the BSA residues of tryptophan over short distances. The results of molecular docking studies indicated that the probable binding location of both dyes is subdomain IB of BSA via hydrophobic interaction and hydrogen bond. Furthermore, as shown by synchronous fluorescence and Fourier transform infrared spectroscopy, both dyes can lead to conformational changes of BSA, which alter its biological functions.Communicated by Ramaswamy H. Sarma.
本研究采用光谱技术和分子对接方法，以阐明牛血清白蛋白（BSA）与两种新合成的偶氮染料之间的相互作用机制。将染料滴定到BSA溶液中会因复合物形成而导致荧光发射猝灭。紫外可见光谱证实，两种染料与BSA在基态形成复合物会引起蛋白质的构象和微环境变化。基于热力学参数的计算，可以得出结论，两种染料均自发结合到BSA上，且范德华力和氢键相互作用在自发结合过程中起主要作用。通过Förster能量转移测量计算了蛋白质与两种染料之间的平均结合距离（r），结果表明两种染料均在短距离内与色氨酸的BSA残基结合。分子对接研究结果表明，两种染料可能的结合位置是通过疏水相互作用和氢键与BSA的亚结构域IB结合。此外，同步荧光和傅里叶变换红外光谱表明，两种染料均可导致BSA的构象变化，从而改变其生物学功能。由Ramaswamy H. Sarma传达。
