• شماره ركورد كنفرانس
    5328
  • عنوان مقاله

    Effect of Cα -methylated residue on the folding behavior of p53 peptide: A Molecular Dynamics Study

  • پديدآورندگان

    Jalili Seifollah sjalili@kntu.ac.ir Department of Chemistry, K. N. Toosi University of Technology, Tehran, Iran , Zarurati Elham elhamzaroorati@yahoo.com Department of Chemistry, K. N. Toosi University of Technology, Tehran, Iran

  • تعداد صفحه
    2
  • كليدواژه
    P53 , Cα , Me , α , residue , Molecular dynamics simulations.
  • سال انتشار
    1400
  • عنوان كنفرانس
    بيست و سومين كنفرانس شيمي فيزيك انجمن شيمي ايران
  • زبان مدرك
    انگليسي
  • چكيده فارسي
    Disorders in protein-protein interactions are often the main cause of several diseases, making them attractive as drug targets. One of the cancer- associated protein -protein interactions is the Hdm2-p53 complex. Over expression of Hdm2 disrupts the normal activity of p53, which is commonly seen in cancer cells containing the p53 normal type. Disruption of the HDM2-p53 interaction to maintain p53 function is considered a therapeutic approach to cancer treatment. To inhibit unnatural PPIs, researchers are always look for strategies that interfere with these interactions. Helix mimetics containing Cα-methylated residues can be a good inhibitor for P53-Hdm2 interaction.
  • كشور
    ايران