In silico and in vitro studies of cytotoxic activity of different peptides derived from vesicular stomatitis virus G protein

Objective(s):This study aims at exploring cytotoxic activity of different peptides derived from VSVG protein against MCF-7 and MDA-MB-231 breast cancer cell lines and human embryonic kidney normal cell (HEK 293).    Materials and Methods: The ANTICP web server was used to predict anticancer peptides. The cytotoxic activity of peptides with high score (P26, P7) and low score (P19) was examined by MTT and DNA fragmentation assays. Results: The results obtained from ANTICP web serverdemonstrated that 4 out of 48 peptides (P26, P7, P10, and P16) had anticancer activity. P26 and P7 peptides of these 4 peptides were detected to have high cytotoxic activity against MCF-7 cells with CC50 values of 98,280 µg/ml and MDA-MB231 cells with CC50 100,550 µg/ml, respectively. In addition, the results showedthat amino acid residues of these 4 peptides were located near fusion domain. Conclusion: The results confirmed that P26 and P7 peptides might induce membrane damage and initiate apoptosis. The present study suggested that P26 and P7 peptides could be appropriate candidates for further studies as cytotoxic agents and modifications in the residue at positions 70-280 might potentially produce a more efficient VSVG protein in gene therapy.

In silico and in vitro studies of cytotoxic activity of different peptides derived from vesicular stomatitis virus G protein Keywords:

ANTICP , Apoptosis , Cytotoxic , Pseudo typing , VSVG protein