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Hydrophobic Interactions Are a Key to MDM2 Inhibition by Polyphenols as Revealed by Molecular Dynamics Simulations and MM/PBSA Free Energy Calculations

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  • Sharad Verma
  • Sonam Grover
  • Chetna Tyagi
  • Sukriti Goyal
  • Salma Jamal
  • Aditi Singh
  • Abhinav Grover

Abstract

p53, a tumor suppressor protein, has been proven to regulate the cell cycle, apoptosis, and DNA repair to prevent malignant transformation. MDM2 regulates activity of p53 and inhibits its binding to DNA. In the present study, we elucidated the MDM2 inhibition potential of polyphenols (Apigenin, Fisetin, Galangin and Luteolin) by MD simulation and MM/PBSA free energy calculations. All polyphenols bind to hydrophobic groove of MDM2 and the binding was found to be stable throughout MD simulation. Luteolin showed the highest negative binding free energy value of -173.80 kJ/mol followed by Fisetin with value of -172.25 kJ/mol. It was found by free energy calculations, that hydrophobic interactions (vdW energy) have major contribution in binding free energy.

Suggested Citation

  • Sharad Verma & Sonam Grover & Chetna Tyagi & Sukriti Goyal & Salma Jamal & Aditi Singh & Abhinav Grover, 2016. "Hydrophobic Interactions Are a Key to MDM2 Inhibition by Polyphenols as Revealed by Molecular Dynamics Simulations and MM/PBSA Free Energy Calculations," PLOS ONE, Public Library of Science, vol. 11(2), pages 1-14, February.
    • Handle: RePEc:plo:pone00:0149014
    DOI: 10.1371/journal.pone.0149014
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    Cited by:

    1. Sharad Verma & Sukriti Goyal & Anchala Kumari & Aditi Singh & Salma Jamal & Abhinav Grover, 2018. "Structural investigations on mechanism of lapatinib resistance caused by HER-2 mutants," PLOS ONE, Public Library of Science, vol. 13(2), pages 1-13, February.

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