@Article{JAMS-4-225,
author = {Chen , JianzhongLiang , Zhi-QiangZhang , Qing-GangLiu , Xiao-YangWang , Wei and Liu , Jin-Qing},
title = {Insight into Interaction Mechanism of the Inhibitor pDI6W with MDM2 Based on Molecular Dynamics},
journal = {Journal of Atomic and Molecular Sciences},
year = {2013},
volume = {4},
number = {3},
pages = {225--234},
abstract = {<p style="text-align: justify;">The p53-MDM2 interaction has been an important target of drug design curing cancers. In this work, Molecular dynamics (MD) simulation coupled with molecular mechanics/Poisson Boltzmann surface area method (MM-PBSA) is performed to
calculate binding free energy of peptide inhibitor pDI6W to MDM2. The results show
that van der Waals energy is the dominant factor of the pDI6W-MDM2 interaction.
Cross-correlation matrix calculated suggests that the main motion of the residues in
MMDM2 induced by the inhibitor binding is anti-correlation motion. The calculations
of residue-residue interactions between pDI6W and MDM2 not only prove that five
residues Phe19’, Trp22’, Trp23’, Leu26’ and Thr27’ from pDI6W can produce strong interactions with MDM2, but also show that $CH$-$π,$ $CH$-$CH$ and $π$−$π$ interactions drive
the binding of pDI6W in the hydrophobic cleft of MDM2. This study can provide theoretical helps for anti-cancer drug designs.</p>},
issn = {2079-7346},
doi = {https://doi.org/10.4208/jmas.063012.072912a},
url = {http://global-sci.org/intro/article_detail/jams/8254.html}
}