Erlista, Garnis Putri and Ahmed, Naseer and Swasono, Respati Tri and Raharjo, Slamet and Raharjo, Tri Joko (2023) Proteome of monocled cobra (Naja kaouthia) venom and potent anti breast cancer peptide from trypsin hydrolyzate of the venom protein. Saudi Pharmaceutical Journal, 31 (6). 1115 – 1124. ISSN 13190164
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Abstract
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 Naja kaouthia 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 N. kaouthia as anticancer. Proteome analysis was employed trypsin hydrolysis of N. kaouthia 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 N. kaouthia 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 N. kaouthia became a potent source of new anticancer agents. © 2023 The Author(s)
Item Type: | Article |
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Additional Information: | Cited by: 0; All Open Access, Gold Open Access, Green Open Access |
Uncontrolled Keywords: | peptide; peptides and proteins; proteome; snake venom; trypsin; unclassified drug; venom protein; amino acid sequence; antineoplastic activity; Article; binding affinity; controlled study; cytotoxicity assay; enzymatic hydrolysis; fractionation; human; human cell; IC50; mass spectrometry; MCF-7 cell line; molecular docking; Naja; Naja kaouthia; nonhuman; protein analysis; protein content; proteomics; selectivity index; ultraviolet visible spectrophotometry; Vero cell line |
Subjects: | Veterinary Medicine |
Divisions: | Faculty of Veterinary Medicine |
Depositing User: | Sri JUNANDI |
Date Deposited: | 31 Oct 2024 05:19 |
Last Modified: | 31 Oct 2024 05:19 |
URI: | https://ir.lib.ugm.ac.id/id/eprint/6067 |