Identification, screening and molecular mechanisms of natural stable angiotensin-converting enzyme (ACE) inhibitory peptides from foxtail millet protein hydrolysates: a combined <i>in silico</i> and <i>in vitro</i> study
Yiqing Zhu, Changyu Chen, Zijian Dai, Han Wang, Yiyun Zhang, Qingyu Zhao, Yong Xue, Qun Shen
Abstract
in ACE to demonstrate its ACE inhibitory activity. The binding of LVPYRP to ACE enhances the rearrangement of ACE's active structural domains, with electrostatic and polar solvation energy contributing the most energy to the binding. Our findings suggested that LVPYRP derived from foxtail millet protein hydrolysates has the potential to be incorporated into functional foods to provide antihypertensive benefits.
Topics & Concepts
FoxtailIn silicoHydrolysateIn vitroEnzymeBiochemistryChemistryPeptideAngiotensin-converting enzymeBiologyGeneHydrolysisBotanyBlood pressureEndocrinologyProtein Hydrolysis and Bioactive PeptidesInsect Utilization and EffectsMeat and Animal Product Quality