In silico identification of antidiabetic and hypotensive potential bioactive peptides from the sheep milk proteins—a molecular docking study. Issue 11 (29th March 2022)

• Record Type: Journal Article
• Authors: Iram, Daraksha; Sansi, Manish Singh; Zanab, Sameena; Vij, Shilpa; Ashutosh, ; Meena, Sunita
• Is Part Of: Journal of food biochemistry. Volume 46:Issue 11(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-03-29
• Subjects: bioactive peptides -- DPP‐IV and ACE inhibitory peptides -- in silico proteolysis -- molecular docking -- sheep milk proteins; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Biochemistry -- Periodicals; 664.024
• DOI: 10.1111/jfbc.14137
• Languages: English
• ISSNs: 0145-8884

Abstract

Abstract: An in silico approach was used for hydrolysis of sheep milk proteins (α‐s1, α‐s2, β‐casein, κ‐Cn, α‐lactalbumin, and β‐lactoglobulin) by gastrointestinal enzymes in order to generate bioactive peptides (BAPs) that can inhibit ACE and DPP‐IV. Sheep milk proteins showed higher similarity with goat milk proteins. These data were acquired via the Clustal Omega tool to perform sequence alignment analysis. The BIOPEP‐UWM database was used to examine the ability of sheep milk protein sequences to generate BAPs, which included a description of their potential bioactivity as well as the frequency of fragments with specified activities. Using the "Enzyme(s) action" tool (BIOPEP‐UWM), digestive enzymes pepsin, trypsin, and chymotrypsin, and three enzyme combinations were selected to computationally hydrolyze milk proteins for obtaining information about ACE and DPP‐IV inhibitory peptides. Other online programs were used to test potential peptides for bioactivity, toxicity, and physicochemical properties. BAPs produced from PTC‐hydrolyzed proteins were analyzed using a peptide ranker, and their inhibitory effects on ACE and DPP‐IV were determined using molecular docking. Consequently, the results of molecular docking analysis show that the peptide PSGAW (αS1‐Cn f155–159) binds to DPP‐IV with binding energy (−8.9 kcal/mol). But in the case of ACE, two potential BAPs were selected: QPPQPL (β‐Cn f161‐166) and PSGAW. These two BAPs revealed a higher binding affinity for ACE with a binding energy of −9.8 kcal/mol. Thus, the results showed that sheep milk proteins were a promising source of antidiabetic and hypotensive peptides. However, experimental and pre‐clinical studies are necessary to assay their therapeutic effects. Practical applications: Sheep milk proteins are known as a high‐quality milk protein resource. Effective enzymatic hydrolysis of sheep milk proteins can release bioactive peptides and also release potential ACE and DPP‐IV inhibitory peptides. This in silico study specifies a theoretical root for sheep milk proteins as a novel source of potential bioactive peptides and may offer guidance for invitro hydrolysis of proteins for the production of bioactive peptides valuable for human consumption. Abstract : Sheep milk intact proteins have the potential to produce various biological peptides. In silico proteolysis of sheep milk proteins using an enzyme combination produced ACE‐I and DPP‐IV inhibitory BAPs. Molecular docking was used to identify BAPs that inhibit ACE‐I and DPP‐IV. An enzyme combination used in silico proteolysis gives guidance for lab‐based protein hydrolysis for the generation of BAPs.