Fig 1.
Docking of C60-16 with acetylcholinesterase: (A) The binding of C60-16 in the active site of acetylcholinesterase. The C60-16 is shown in stick model while the surface of acetylcholinesterase is shown in green, blue and purple (B) The three dimensional analysis of the interactions of C60-16 in the active site of acetylcholinesterase.
The C60-16 makes interactions with Tyr67, Trp81, Gly114, Tyr118, Ser119, Gly120, Tyr127, Trp276, Phe327 and Tyr331.
Fig 2.
Docking of C60-11 with glutamate racemase: (A) The binding of C60-11 in the active site of glutamate racemase. The C60-11 is shown in stick model while glutamate racemase is shown in surface model (B) The interactions between C60-11 and glutamate racemase.
The C60-11 makes interactions with Cys70, Cys178, His180, Tyr181, Leu184, Lys185, Lys186, Leu234, Leu237 and Ile238. The distances between interacting atoms are shown in angstroms.
Fig 3.
Docking of C60-10 and C60-16 with inosine monophosphate dehydrogenase: (A) The binding patterns of C60-10 and C60-16 in the active site of inosine monophosphate dehydrogenase. The C60-10 and C60-16 are shown in stick model with golden and blue color respectively while the surface of inosine monophosphate dehydrogenase is shown in green, blue and purple (B) The analysis of interactions of C60-16 in the active site of inosine monophosphate dehydrogenase.
The C60-16 makes contacts with Asn239, Arg241, Ser317, Ile318, Cys319, Gly381, Arg382, Tyr383, Tyr405, Gly409, Arg414, Trp416 and Glu431. The contacts are marked as lines and the distances between interacting atoms are shown in angstroms.
Fig 4.
Docking of C60-16 and C60-11 with lumazine synthase: (A) The binding of C60-16 and C60-11 in the active site of lumazine synthase. The C60-16 and C60-11 are shown in sticks with blue and golden color respectively while the surface of lumazine synthase is shown in green, blue and purple (B) The interactions of C60-16 in the active site of lumazine synthase.
The C60-16 makes interactions with the resides from chain A Asn114’, Val116’, Arg128’, Lys138’ and from chain B Trp27, His28, Ala59, His89, Val82, Ile83. The distances of various atoms are marked as thin lines and shown in angstroms.
Fig 5.
Docking of C60-16 with human estrogen receptor alpha: (A) The binding of C60-16 in the active site of human estrogen receptor alpha. The C60-16 is shown in stick while the surface of human estrogen receptor alpha is shown in green, blue and purple (B) The three dimensional analysis of the interactions of C60-16 in the active site of human estrogen receptor alpha.
The C60-16 makes interactions with Asp351, Leu384, Trp383, Ile424, Leu525, Cys530, Val533, Val534 and Leu539. The distances between various atoms are marked as thin lines.
Fig 6.
Docking of C60-10 with dihydrofolate reductase: (A) The binding pattern of C60-10 in the active site of dihydrofolate reductase. The C60-10 is shown in stick while dihydrofolate reductase is shown in surface model (B) The diagram of the interactions bewteeen C60-10 and dihydrofolate reductase.
The C60-10 makes interactions with Leu29, Lys30, Ile51, Lys53, Leu55, Arg58 and Lys145. The hydrogen bonds are shown in thin lines.
Fig 7.
Docking of C60-12 with N-Myristoyltransferase: (A) The binding of C60-12 in the active site of N-Myristoyltransferase. The C60-12 is shown in stick model while the surface of N-Myristoyltransferase is shown in green, blue and purple (B) The analysis of the interactions between C60-12 and N-Myristoyltransferase.
The C60-12 makes interactions with Glu105, Ala109, Ile208, Phe111, Tyr219 and Asp233.
Fig 8.
The molecular dynamics simulation of the C60 derivative/protein complexes: All the complexes are simulated over a period of 25 ns.
The RMSD of the simulation was plotted against time, according to the simulation trajectories.
Fig 9.
The structural superposition of C60 derivative/protein complexes: The initial structures at time = 0ns and final structures after MD simulation (25ns) for all complexes are superposed.
The initial structures are colored in cyan and the final structures are colored in green.