Bioactive peptides derived from the enzymatic hydrolysis of cowhide collagen for the potential treatment of atherosclerosis: A computational approach

作者：Mamoudou Hamadou, Bahri Başaran, Martin Alain Mune Mune, Abdulhalim Musa Abubakar, Jairus Olumasai Nandwa, Mouhamed Zakiou Kolawole Adissa Raimi, Muhammad Zaffar Hashmi · 发表于：Intelligent Pharmacy · 年份：2024 · DOI：10.1016/j.ipha.2024.05.004 · 被引用次数：23 · 研究领域：Protein Hydrolysis and Bioactive Peptides、Computational Drug Discovery Methods、Meat and Animal Product Quality

Cowhide collagen hydrolysates (CCHs) are peptides and amino acids obtained from the partial hydrolysis of collagen. These have numerous potential applications in the food, biomedical, and pharmaceutical industries. The study analyzed the physicochemical, antioxidant, and anti-atherosclerosis properties of collagen hydrolysates (CCHs) from cowhide using in silico methods. Proteins were identified in silico based on their molecular weights and origin from the protein database (UniProtKB). Using bioinformatics tools, numerous physicochemical properties (toxicity and amino acid composition) were determined. The identified proteins were subsequently subjected to an in silico enzymatic hydrolysis using pepsin, thermolysin, and proteinase K. The peptides obtained were characterized. Molecular docking was conducted between the peptides generated in silico and the three target enzymes (3-Hydroxy-3-Methylglutaryl-CoA (HMG-CoA) reductase, cyclooxygenase-2, and Nicotinamide Adenine Dinucleotide Phosphate (NADPH) oxidase). Two cowhide collagens were identified, F1MJQ6 and G3MZI7, with molecular weights of 172,076 and 184,867 Dalton, respectively. A compositional analysis of F1MJQ6 and G3MZI7 revealed the significant presence of glycine residues at 25% and 23%, and proline residues at 16% and 18%, respectively. The G3MZI7 and F1MJQ6 proteins exhibited a high concentration of both essential and semi-essential amino acids. The molecular docking results indicate that the antioxidant peptides ...