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
كليدواژه :
P53 , Cα , Me , α , residue , Molecular dynamics simulations.
عنوان كنفرانس :
بيست و سومين كنفرانس شيمي فيزيك انجمن شيمي ايران
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.
