Yang Sheng-Tao, Wang Haifang, Guo Lin, Gao Yang, Liu Yuanfang, Cao Aoneng
Beijing National Laboratory for Molecular Sciences; Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, People's Republic of China.
Nanotechnology. 2008 Oct 1;19(39):395101. doi: 10.1088/0957-4484/19/39/395101. Epub 2008 Aug 8.
The potential biomedical applications of fullerenol C(60)(OH)(x) (x≈24) have been extensively studied. However, the structural information of the interaction of fullerenol with the bio-system at the molecular level, which is essential for understanding its bioactivity and toxicity, is still missing. In this study, lysozyme was selected as a model protein to investigate the interaction between fullerenol and biomolecules. A strong induced circular dichroism (CD) signal of achiral fullerenol was observed after binding with lysozyme. Activity assay shows that lysozyme activity is inhibited significantly by fullerenol. No heat capacity difference between the folded and unfolded states of lysozyme was measured by differential scanning calorimetry (DSC) in the presence of fullerenol, indicating that fullerenol prefers to bind with the hydrophobic residues. Both experimental and Autodock computational results suggest that the binding site on lysozyme for fullerenol is close to Trp 62, and a π-π stacking interaction might play an important role in binding.
富勒醇C(60)(OH)(x)（x≈24）的潜在生物医学应用已得到广泛研究。然而，对于理解其生物活性和毒性至关重要的富勒醇与生物系统在分子水平上相互作用的结构信息仍然缺失。在本研究中，选择溶菌酶作为模型蛋白来研究富勒醇与生物分子之间的相互作用。与溶菌酶结合后，观察到非手性富勒醇有强烈的诱导圆二色性（CD）信号。活性测定表明，富勒醇可显著抑制溶菌酶活性。在有富勒醇存在的情况下，通过差示扫描量热法（DSC）未测得溶菌酶折叠态与未折叠态之间的热容量差异，这表明富勒醇更倾向于与疏水残基结合。实验和自动对接计算结果均表明，溶菌酶上富勒醇的结合位点靠近色氨酸62，并且π-π堆积相互作用可能在结合中起重要作用。
