eng URI http://hdl.handle.net/10795/2605 βιοχημεία ένζυμο βιοτεχνολογία Glutathione S-transferases catalyze the conjugation of glutathione (GSH) to a variety of hydrophobic substrates, rendering them hydrophilic and facilitating their metabolic processing and secretion from the cell. GSTs are involved in major detoxification mechanisms of the cell from several xenobiotics and drugs. On the other hand, on the basis of the same detoxification mechanisms, cancer cells may acquire resistance by overexpressing GST activities, thus hampering the effectiveness of certain chemotherapeutic drugs and leading to chemotherapeutic resistant tumor cells. Several synthetic drugs and prodrugs exhibiting inhibition potency against GSTs have been proposed as strategies to overcoming multiple drug resistance (MDR) attributed to GST overexpression. In the pursuit of identifying new lead compounds as inhibitors against hGSTs involved in MDR we have used Structure Based Ligand Design techniques to generate in silico xanthone and benzophenone derivatives and performed extensive molecular docking and binding evaluation on the structure of hGSTA1-1. 1 pp. LOMv1.0 creator LOMv1.0 Project Final Beneficiary LOMv1.0 Project Executing Organisation 2015 Digital Library of the Operational Programme "Education and Lifelong Learning" abstract types Text Human glutathione transferase Multiple drug resistance MDR In silico design Xanthone analogues In silico design 1313477 application/pdf http://repository.edulll.gr/edulll/bitstream/10795/2605/2/2605_Poster%205.pdf URI http://hdl.handle.net/10795/2605 LOMv1.0creator 2016-04-13T10:39:28Z LOMv1.0validator 2016-04-13T10:39:28Z LOMv1.0 gre no no Copyright EYD-EPEDBM (Operational Programme "Education and Lifelong Learning")