Proceedings of the 3rd International Conference on Computation for Science and Technology

Molecular Docking and Molecular Dynamics Simulation of the Interaction of Cationic Imidazolium Porphyrin-Anthraquinone and Hsp90

Muhammad Arba, Rahmana Emran Kartasasmita, Daryono H. Tjahjono
Corresponding author
Cationic porphyrin, Hsp90, MM-PBSA, in silico, molecular docking, molecular dynamics simulation
Hsp90 is involved in the progressiveness of cancer cell through the activation of oncogenic client proteins, including Her2/ErbB2, Akt, Raf-1, and hTERT. Thus, targeting Hsp90 is considered as one of promising strategy in anti-cancer drug development. In the search of new potential Hsp90 inhibitors, three cationic imidazolium porphyrin-anthraquinone have been designed and their binding mode and affinity to Hsp90 were calculated employing AutoDock 4.2 and MM-PBSA method. All three ligands well fit into the binding site of Hsp90 and were able to interact with Hsp90 through hydrogen bond and additional -cationic interactions, in which the latter was absent in the interaction of geldanamycin (GD). Molecular dynamics simulation confirmed the stability of each complex, and prediction of binding affinity using MM-PBSA method show that porphyrin hybrids have comparable binding energies with that of GD.
Download article (PDF)