In Silico Study of Desmosdumotin as an Anticancer Agent: Homology Modeling, Docking and Molecular Dynamics Simulation Approach

ISSN: 1875-5992 (Online)
ISSN: 1871-5206 (Print)

Volume 17, 14 Issues, 2017

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Anti-Cancer Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Cancer Agents

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Michelle Prudhomme
Institut de Chimie de Clermont-Ferrand
Université Clermont Auvergne

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In Silico Study of Desmosdumotin as an Anticancer Agent: Homology Modeling, Docking and Molecular Dynamics Simulation Approach

Anti-Cancer Agents in Medicinal Chemistry, 13(10): 1636-1644.

Author(s): Changdev G. Gadhe, Gugan Kothandan and Seung Joo Cho.

Affiliation: College of Medicine, Chosun University, 375 Seosuk-dong, Dong-gu Gwangju 501-759, Republic of Korea.


P-glycoprotein (P-gp) is responsible for the multidrug resistance (MDR) and involved in the expulsion of xenobiotics out of cell. In this paper, homology modeling, docking and molecular dynamics simulation (MDS) was performed for the human P-gp desmosdumotin inhibitor. Docking study was carried out in the P-gp nucleotide binding domain 2 (NBD2). The desmosdumotin binding region occupied the ATP binding region (flavonoid binding region) with hydrophobic and hydrophilic interactions. Analysis of root mean square deviations (RMSDs) of active site residues indicated the binding site residues were stable throughout the simulation period. As shown in previous results with structurally similar flavonoid compounds, van der Waals and electrostatic interactions were found to be important factors for the desmosdumotin-NBD2 inhibition. Docking results suggest that desmosdumotin interacts with the NBD2 through both hydrogen bonds (Lys1076, Ser1077 and Thr1078) and hydrophobic interactions (Tyr1044, Val1052, Gly1073 and Cys1074). In addition, the involvement of other amino-acids was identified via MDS (Lys1076 and Ser1077 for hydrogen bonds and Tyr1044, Val1052, Gly1073, Cys1074 and Gly1075 for hydrophobic interactions). Thus, current preliminary model of interactions between desmosdumotin-NBD2 could be helpful to understand the in-depth inhibition mechanism of P-gp at NBD2 level and to design more potent inhibitors which could effectively overcome MDR of anticancer agents.


Anti-cancer agent, desmosdumotin, docking, dynamic simulation, homology modeling, NBD2, P-gp.

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Article Details

Volume: 13
Issue Number: 10
First Page: 1636
Last Page: 1644
Page Count: 9
DOI: 10.2174/18715206113139990302
Price: $58
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