In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RBC, including RBC7 (TPYPCV), RBC15 (VVYPWR) and RBC9 (FLCT), showed IC50 values of 2.58 +/- 0.87, 5.22 +/- 2.56 and 6.53 +/- 0.34 mu m, respectively. By comparison, PL1 (YTFPFH), PL2 (WGHGNPHV) and PL7 (VPLW) from PL displayed higher IC50 values at 24.12 +/- 2.44, 15.33 +/- 0.44 and 32.80 +/- 38.96 mu m, respectively. Molecular docking was employed to simulate the interactions of RBC7 and RBC15 with the catalytic site of the ACE receptor. RBC7 and RBC15 interacted with residues in the ACE receptor that normally coordinated with Zn(II), and RBC7 also interacted extensively with residues within S1, S2 and S'1 active sites. Taken together, these results illustrate that porcine blood is an excellent source of antihypertensive peptides and could be of great benefits to people with high blood pressure.

Automated summary

New bioactive peptides with antihypertensive properties were identified from porcine blood, showing potential in the treatment of high blood pressure.