Proteome of monocled cobra ( venom and potent anti breast cancer peptide from trypsin hydrolyzate of the venom protein.

Anticancer peptide is one of the target in the development of new anticancer drug. Bioactive peptide can be originated from isolated free peptide or produced by hydrolysis of protein. Protein is the main component of venom, and due to the toxicity of the venom, it can be assessed as the source of anticancer peptides. This study aims to characterize the venom protein and to identify peptides from the snake venom of as anticancer. Proteome analysis was employed trypsin hydrolysis of venom protein completed with HRMS analysis protein database query. Preparative tryptic hydrolysis of the protein followed by reverse-phased fractionation and anti breast cancer activity testing were performed to identify the potent anticancer from the hydrolysate. Proteomic analysis by high-resolution mass spectrometry revealed that there are 20 enzymatic and non-enzymatic proteins in venom. The 25% methanol peptide fraction had the most active anticancer activity against MCF-7 breast cancer cells and showed promising selectivity (selectivity index = 12.87). Amino acid sequences of eight peptides were identified as potentially providing anticancer compounds. Molecular docking analysis showed that WWSDHR and IWDTIEK peptides gave specific interactions and better binding affinity energy with values of -9.3 kcal/mol and -8.4 kcal/mol, respectively. This study revealed peptides from the snake venom of became a potent source of new anticancer agents.