Analyses of the Binding between Water Soluble C60 Derivatives and Potential Drug Targets through a Molecular Docking Approach

• Published in: PloS one 2016-02, Vol.11 (2), p.e0147761-e0147761
• Main Authors: Junaid, Muhammad, Almuqri, Eman Abdullah, Liu, Junjun, Zhang, Houjin
• Format: Article
• Language: English
• Subjects: Acetylcholinesterase; Acetylcholinesterase - chemistry; Acyltransferases - chemistry; Amino Acid Isomerases - chemistry; Analysis; Binding sites; Biology and Life Sciences; Biotechnology; Buckminsterfullerene; Chemical properties; Chemistry; Derivatives; Dihydrofolate reductase; Drug discovery; Drug dosages; Estrogen Receptor alpha - chemistry; Estrogens; Fullerenes; Fullerenes - chemistry; Gene expression; Glutamate racemase; Humans; IMP Dehydrogenase - chemistry; Inhibitors; Inosine monophosphate; Kinases; Life sciences; Ligands; Lumazine synthase; Medicine and Health Sciences; Molecular biology; Molecular docking; Molecular Docking Simulation; Molecular Dynamics Simulation; Molecular modeling; Multienzyme Complexes - chemistry; N-Myristoyltransferase; Organic solvents; Pharmaceutical Preparations - chemistry; Physical Sciences; Physiological aspects; Proteins; Rodents; Solubility; Solvents; Studies; Tetrahydrofolate Dehydrogenase - chemistry; Tropical diseases; Water - chemistry
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0147761

Fullerene C60, a unique sphere-shaped molecule consisting of carbon, has been proved to have inhibitory effects on many diseases. However, the applications of C60 in medicine have been severely hindered by its complete insolubility in water and low solubility in almost all organic solvents. In this study, the water-soluble C60 derivatives and the C60 binding protein's structures were collected from the literature. The selected proteins fall into several groups, including acetylcholinesterase, glutamate racemase, inosine monophosphate dehydrogenase, lumazine synthase, human estrogen receptor alpha, dihydrofolate reductase and N-myristoyltransferase. The C60 derivatives were docked into the binding sites in the proteins. The binding affinities of the C60 derivatives were calculated. The bindings between proteins and their known inhibitors or native ligands were also characterized in the same way. The results show that C60 derivatives form good interactions with the binding sites of different protein targets. In many cases, the binding affinities of C60 derivatives are better than those of known inhibitors and native ligands. This study demonstrates the interaction patterns of C60 derivatives and their binding partners, which will have good impact on the fullerene-based drug discovery.