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

DOI

10.2991/iccst-15.2015.1How to use a DOI?

Keywords

Cationic porphyrin, Hsp90, MM-PBSA, in silico, molecular docking, molecular dynamics simulation

Abstract

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.

Copyright

© 2015, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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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  - 10.2991/iccst-15.2015.1
ID  - Arba2015/01
ER  -