Quantitative sequence-activity modeling of ACE peptide originated from milk using ACC-QTMS amino acid indices.

Up to now, numerous peptides/hydrolysates derived from casein and whey protein have shown angiotensin-I-converting enzyme (ACE) inhibitory. In this research, quantum topological molecular similarity (QTMS) indices of amino acids were utilized in quantitative sequence-activity modeling (QSAM) to predict the activity of a set of milk-driven peptides with ACE inhibition. Since the derived peptides have not the same number of residues, we overcame this issue by auto cross covariance (ACC) methodology. Then, some QSAMs were built to predict the pIC50 value of ACE peptides derived from Bovine Casein and Whey. The model established an acceptable relationship between the selected variables and the pIC50 of the peptides. To estimate the performance of the developed models, casein and whey proteins from human, goat, bovine and sheep were virtually broken by trypsin and chymotrypsin enzymes and the ACE activity of the resultant virtual peptides were predicted and some new ACE peptides were proposed.