Intensifying the Anticancer Potential of Cationic Peptide Derived from Serine Threonine Protein Kinase of Teleost by Tagging with Oligo Tryptophan

Abstract

Serine threonine protein kinase plays an important role in the cell growth, cell cycle regulation and development which shows a significant role in signal transduction pathway. In this study, a cationic peptide IE13 was derived from serine threonine protein kinase of a teleost fish and it was modified as IW13 by replacing the C-terminal residue with tryptophan. The anticancer potential of IE13 and IW13 was tested against three different types of cell lines HeLa (Human Cervical carcinoma cells), A549 (Human lung cancer cells) and MCF 7 (Human breast cancer cells) at different concentrations (300, 100, 30 and 10 µM) in semi logarithmic range. The results showed that the peptide IW13 showed EC50 of 92 µM for MCF 7, 102 µM for A549 and 85 µM for HeLa whereas, IE13 showed less growth inhibition on the tested cell lines. The flow cytometry study was conducted to demonstrate the cell cycle inhibition by the cationic peptide IW13 against HeLa cell line. Cytotoxicity studies of the cationic peptide showed no cytotoxicity against normal cell line (RAW 264.7). Tailoring of these properties was likely to be a key in safe and successful transfer of this peptide from laboratory experiments into clinical practice for pharmaceutical formulations.