Lichota Anna, Szabelski Mariusz, Krokosz Anita
Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, 90-236 Lodz, Poland.
Department of Physics and Biophysics, Faculty of Food Science, University of Warmia and Mazury in Olsztyn, 10-719 Olsztyn, Poland.
Int J Mol Sci. 2022 Oct 16;23(20):12382. doi: 10.3390/ijms232012382.
The effect of the interaction between fullerenol C(OH) (FUL) and alcohol dehydrogenase (ADH) from and human serum albumin (HSA) was studied by absorption spectroscopy, fluorescence spectroscopy, and time-resolved fluorescence spectroscopy. As shown in the study, the fluorescence intensities of ADH and HSA at excitation wavelengths λ = 280 nm (Trp, Tyr) and λ = 295 nm (Trp) are decreased with the increase in the FUL concentration. The results of time-resolved measurements indicate that both quenching mechanisms, dynamic and static, are present. The binding constant K and the number of binding sites were obtained for HSA and ADH. Thus, the results indicated the formation of FUL complexes and proteins. However, the binding of FUL to HSA is much stronger than that of ADH. The transfer of energy from the protein to FUL was also proved.
通过吸收光谱、荧光光谱和时间分辨荧光光谱研究了富勒醇C(OH)（FUL）与来自[具体来源未给出]的乙醇脱氢酶（ADH）和人血清白蛋白（HSA）之间相互作用的影响。研究表明，在激发波长λ = 280 nm（色氨酸、酪氨酸）和λ = 295 nm（色氨酸）处，ADH和HSA的荧光强度随着FUL浓度的增加而降低。时间分辨测量结果表明，动态猝灭和静态猝灭机制均存在。获得了HSA和ADH的结合常数K和结合位点数。因此，结果表明形成了FUL与蛋白质的复合物。然而，FUL与HSA的结合比与ADH的结合要强得多。还证明了能量从蛋白质转移到FUL。
