1. Interaction of peptides selected from artificial peptide library with doxorubicin resistant K562 cells
- Author
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Erol Ömer Atalay, Sanem Arikan, and Ayfer Atalay
- Subjects
K562-dox cells ,Cancer Research ,Cell viability ,phage KPB7 ,phage KPB10 ,DNA sequence ,Peptide libraries ,animal cell ,doxorubicin ,peptide library ,cell strain K 562 ,phage KPP8 ,bacteriophage ,physical chemistry ,controlled study ,protein interaction ,Peptide library ,biopanning ,hydrophobicity ,Doxorubicin resistant ,nonhuman ,Chemistry ,article ,molecular library ,nucleotide sequence ,cell clone ,Combinatorial chemistry ,DNA isolation ,Oncology ,Biochemistry ,Xtt assay ,cell function ,Phage display ,K562 cells ,cell structure - Abstract
The ability of a peptide to target a specific protein in vitro has a potential for recognizing the cell membrane structure, protein-protein and receptor-ligand interaction. On the basis of molecular interactions, cell specific peptides were selected via phage library approach and their functions on the cells were determined by XTT based viability assay. We aimed to find phage displayed peptides from 12-mer peptide library that interact with K562-dox cell membrane in association with cellular functions and to study the effects of peptides selected from artificial peptide library on K562-dox cell viability. Peptides recognizing K562-dox cells were identified according to peptide sequences and amino acid properties. We selected 29 different phages from biopannings with K562-dox cells. Three clones were identified (KPB7,KPB10, KPP8) and their negative effects on cell viability were determined by XTT assay. According to our cell viability assay results, selected phages were effected negatively to the viability of the K562-dox cells. Depending on the present results, peptides were obtained that could be potential candidates for molecular recognition and cell targeting approaches. © 2010 Academic Journals Inc.
- Published
- 2010