Dipartimento di Chimica "G. Ciamician", Universita' di Bologna, V. F. Selmi 2, 40126 Bologna, Italy.
ACS Nano. 2010 Apr 27;4(4):2283-99. doi: 10.1021/nn901809b.
About 20 proteins are known to modify their activity upon interaction with C60. Their structures are present in a database that includes more than 1200 protein structures selected as possible targets for drugs and to represent the entire Protein Data Bank. The set was examined with an algorithm that appraises quantitatively the interaction of C60 and the surface of each protein. The redundancy of the set allows to establish the predictive power of the approach that finds explicitly the most probable site where C60 docks on each protein. About 80% of the known fullerene binding proteins fall in the top 10% of scorers. The close match between the model and experiments vouches for the accuracy of the model and validates its predictions. The sites of docking are shown and discussed in view of the existing experimental data available for protein-C60 interaction. A closer exam of the 10 top scorers is discussed in detail. New proteins that can interact with C60 are identified and discussed for possible future applications as drug targets and fullerene derivatives bioconjugate materials.
已知约有 20 种蛋白质在与 C60 相互作用时会改变其活性。这些蛋白质的结构都包含在一个数据库中，该数据库包含了 1200 多种被选为药物靶点的蛋白质结构，以代表整个蛋白质数据库。该集合使用一种算法进行了检查，该算法定量评估了 C60 与每个蛋白质表面的相互作用。集合的冗余性允许建立该方法的预测能力，该方法可以明确找到 C60 在每个蛋白质上最可能结合的位点。大约 80%的已知富勒烯结合蛋白属于得分最高的前 10%。模型与实验之间的紧密匹配证明了模型的准确性，并验证了其预测。 docking 的位点根据现有关于蛋白质-C60 相互作用的实验数据进行了显示和讨论。对前 10 名得分最高的进行了更详细的讨论。还确定了可能与 C60 相互作用的新蛋白质，并讨论了它们作为药物靶点和富勒烯衍生物生物缀合物材料的可能未来应用。
