Peptides selected from artificial peptide libraries have special interest in cell targeting, drug discovery, molecular diagnosis and multidrug reversal. Peptides selected from artificial peptide libraries against doxorubicin resistant K562 cells have the capacity in the reversal of the doxorubicin resistance. Our aim is to determine the characteristics of these peptides on recombinant human P-glycoprotein membrane fractions to be able to understand their interactions. Peptides were selected against doxorubicin resistant K562 cells. The effects of synthesized peptides on these cells viability was done by XTT viability assay. The interactions of peptides with P-glycoprotein were done by Pgp-GloTM Assay System by measuring the ATPase activity of P-glycoprotein. According to our results; four selected peptides effected on doxorubicin resistant K562 cells viability and stimulated the P-glycoprotein activity in the presence of doxorubicin at different levels. If the P-glycoprotein stimulation occurs on living doxorubicin resistant K562 cells, cell viability will not be affected due to multidrug resistance effect of P-glycoprotein. Peptides selected from artificial peptide libraries are useful tools in the reversal of multidrug resistance and for understanding the membrane structure-function relationships.
Key words: Recombinant peptides, multidrug resistance, Pp-glycoprotein, membrane biophysics
|
