Molecular Docking and Molecular Dynamics Simulation of the Interaction of Cationic Imidazolium Porphyrin-Anthraquinone and Hsp90
Muhammad Arba, Rahmana Emran Kartasasmita, Daryono H. Tjahjono
Available Online January 2015.
- https://doi.org/10.2991/iccst-15.2015.1How to use a DOI?
- 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.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Muhammad Arba AU - Rahmana Emran Kartasasmita AU - Daryono H. Tjahjono PY - 2015/01 DA - 2015/01 TI - Molecular Docking and Molecular Dynamics Simulation of the Interaction of Cationic Imidazolium Porphyrin-Anthraquinone and Hsp90 BT - Proceedings of the 3rd International Conference on Computation for Science and Technology PB - Atlantis Press SP - 1 EP - 5 SN - 2352-538X UR - https://doi.org/10.2991/iccst-15.2015.1 DO - https://doi.org/10.2991/iccst-15.2015.1 ID - Arba2015/01 ER -