C-terminal sequence deletion effect on antioxidative characteristics of VLPVPQK bioactive peptide from buffalo milk casein. (February 2020)

• Record Type: Journal Article
• Authors: Devi, Savita; Pal, Gaurav Kumar; Kapila, Rajeev; Kapila, Suman
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 119(2020)
• Publication Date: 2020-02
• Subjects: Peptide -- Anti-oxidative -- Fibroblasts -- Oxidative stress -- Hydrogen peroxide; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2019.108816
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: In the recent time, demand for nontoxic antioxidative substances such as peptides has boomed among pharmacologists. In the present investigation, peptides, VLPVPQ and VLPVP were generated from parent antioxidative peptide, VLPVPQK. Initially, all these peptides were studied in-silico for biophysical properties like hydrophobicity, structure, Extinction coefficient, isoelectric point, grand average hydropathy value and Wimley White whole residue hydrophobicity. Inspite of this, homology relationship among organisms, taxonomy, digestibility assessment for proteases, solubility, melting temperature index, half-life time in-vitro and in-vivo, instability index and aliphatic index was compared in-silico . Further, based on these properties, VLPVP was compared with parent peptide, VLPVPQK for antioxidative potential. VLPVP exhibited lesser antioxidative potential by chemical method and in-vitro hydrogen peroxide induced oxidative stress conditions generated in fibroblast cells compared to VLPVPQK. The proliferative potential, cell injury marker, nitric oxide production and pro-inflammatory, Tumor Necrosis Factor-α was measured to compare cytoprotective antioxidative potential. The results displayed the cytoprotective potential of VLPVPQK. In addition, the present study suggested that glutamine and lysine are responsible for the c-terminal sequence based response and cytoprotective potential of milk bioactive peptide, VLPVPQK. Other than this, hydrophobic amino acids and positive charge of the VLPVPQK is also responsible for the cytoprotective potential. Highlights: Milk derived bioactive peptide, VLPVPQK possesses cytoprotective potential. Deletion of glutamine and lysine from the peptide results in loss of cytoprotective potential. Cytoprotective potential of peptide was due to positive charge of the peptide. The present study provides a novel way to design antioxidative peptide as a drug.