Blood pressure regulatory effect of enzyme-assisted hydrolysate from Parapristipoma trilineatum by regulation of angiotensin II and ACE: Identification of ACE inhibition through in silico molecular docking

This study investigated the blood pressure-regulating effects of a pepsin-assisted hydrolysate from Parapristipoma trilineatum (PepH) through both in vitro and in vivo studies. P. trilineatum was hydrolyzed with deionized water and three enzymes (α-chymotrypsin, trypsin, and pepsin). After enzymatic hydrolysis, the ACE inhibitory potential of the hydrolysates was evaluated. Among them, PepH exhibited the strongest ACE inhibitory activity, leading to its selection for subsequent in vivo studies. PepH administration significantly reduced systolic blood pressure and ameliorated hypertension-induced tissue damage in the aorta and heart. Furthermore, PepH significantly decreased serum Angiotensin II (Ang II) and Angiotensin-Converting Enzyme (ACE) levels. Furthermore, in silico molecular docking confirmed that purified peptides strongly bound to the active site of ACE. Collectively, our results suggest that PepH lowers blood pressure and protects against hypertension-induced tissue damage in SHRs. PepH shows potential as a functional food for managing hypertension and preventing related tissue damage. • PepH showed strong ACE inhibitory activity. • PepH administration significantly reduced blood pressure in SHR. • PepH highly regulates the serum Ang II and ACE in SHR. • Purified peptides from PepH exhibited strong binding affinities to ACE, suggesting their potential as ACE inhibitors.