Yang Li-Yun, Hua Si-Yu, Zhou Zhi-Qiang, Wang Guan-Chao, Jiang Feng-Lei, Liu Yi
State Key Laboratory of Virology and Key Laboratory of Analytical Chemistry for Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China; College of Chemistry and Material Sciences, Guangxi Teachers Education University, Nanning 530001, PR China.
State Key Laboratory of Virology and Key Laboratory of Analytical Chemistry for Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Colloids Surf B Biointerfaces. 2017 Sep 1;157:261-267. doi: 10.1016/j.colsurfb.2017.05.065. Epub 2017 May 31.
Fullerenols, known as polyhydroxylated derivatives of fullerene, have attracted great attention due to their distinctive material properties and potential applications in biology and medicine. As a step toward the elucidation of basic behavior in biological systems, a variety of spectroscopic measurements as well as isothermal titration calorimetry (ITC) were applied to study the interaction between fullerenol (C(OH)) and serum proteins (bovine serum albumin (BSA) and γ-globulins). The results of fluorescence spectra indicated that the intrinsic fluorescence of proteins could be effectively quenched by the dynamic mechanism. The affinity values of both proteins bound to fullerenol were of the same order of magnitude. Meanwhile, ITC results showed that the interaction between fullerenol and BSA was enthalpy favorable, while the interaction with γ-globulins was enthalpy unfavorable. Furthermore, fullerenol had little influence on the secondary structure of both proteins. Additional cytotoxicity tests showed that the presence of proteins attenuated the toxic effect of fullerenol on human normal gastric epithelial cell line (GES-1). Thus, the interaction between fullerenol and proteins is indispensable to evaluate the biosafety of fullerenol, which may in turn promotes the development of its biological applications.
富勒醇，即富勒烯的多羟基化衍生物，因其独特的材料特性以及在生物学和医学中的潜在应用而备受关注。作为阐明其在生物系统中基本行为的一步，我们采用了多种光谱测量方法以及等温滴定量热法（ITC）来研究富勒醇（C(OH)）与血清蛋白（牛血清白蛋白（BSA）和γ-球蛋白）之间的相互作用。荧光光谱结果表明，蛋白质的固有荧光可通过动态机制被有效猝灭。两种蛋白质与富勒醇结合的亲和力值处于同一数量级。同时，ITC结果显示富勒醇与BSA的相互作用是焓有利的，而与γ-球蛋白的相互作用是焓不利的。此外，富勒醇对两种蛋白质的二级结构影响很小。额外的细胞毒性测试表明，蛋白质的存在减弱了富勒醇对人正常胃上皮细胞系（GES-1）的毒性作用。因此，富勒醇与蛋白质之间的相互作用对于评估富勒醇的生物安全性不可或缺，这反过来可能会促进其生物学应用的发展。
