Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)

• Published in: Health science reports Vol. 1; no. 1; pp. e17 - n/a
• Main Authors: Komolafe, Kayode, Akinmoladun, Afolabi C., Komolafe, Titilope R., Olaleye, Mary T., Boligon, Aline A., Akindahunsi, Akintunde A., Rocha, Joao B.T.
• Format: Journal Article
• Language: English
• Published: United States John Wiley & Sons, Inc 01.01.2018; John Wiley and Sons Inc
• Subjects: angiotensin‐converting enzyme; Antioxidants; Blood; Enzymes; Flavonoids; hypotensive; Laboratory animals; Leaves; Original Paper; Original Papers; Oxidative stress; P biglobosa; phenolics; Phenols; Phytochemicals; Polyphenols; Nigeria; United States > US; hypotensive; angiotensin‐converting enzyme; P biglobosa; phenolics
• ISSN: 2398-8835; 2398-8835
• DOI: 10.1002/hsr2.17

Aims To investigate the antioxidant activities and effects of free phenols (FPPB) and bound phenols (BPPB) of Parkia biglobosa leaves on some enzymes of neuro‐cardiovascular relevance. Methods and Results HPLC‐DAD fingerprinting of FPPB and BPPB, and the antihemolytic, radical (1,1‐diphenyl‐2 picrylhydrazyl, DPPH; 2,2‐azino‐bis(3‐ethylbenzthiazoline‐6‐sulphonic acid), ABTS) scavenging and ferric reducing antioxidant properties of extracts, were assessed. In addition, the effects of the phenolics on angiotensin‐1‐converting enzyme (ACE), cerebral acetylcholinesterase/butyrylcholinesterase (AChE/BuChE), and Na+/K+ATPase were determined in vitro. FPPB was more potent than BPPB in terms of ABTS (EC50:4.06 ± 0.3 vs 24.07 ± 2.1 μg/mL) and DPPH (EC50:3.82 ± 0.2 vs 10.22 ± 0.1 μg/mL) radicals scavenged, respectively. The free phenolic extract was a better DPPH. scavenger than ascorbic acid (EC50 = 12.58 ± 0.4 μg/mL; DPPH reference) and compared well with Trolox (EC50:4.44 ± 0.08 μg/mL; ABTS reference). The anti‐hemolytic effect of FPPB (36%) and BPPB (53%) was highest at 15 μg/mL but lower than that recorded for ascorbic acid (67% at 10 μg/mL). Even though FPPB (IC50 = 15.35 ± 4.0 μg/mL) and BPPB (IC50 = 46.85 ± 3.3 μg/mL) showed considerably lower ACE‐inhibitory effect than ramipril (IC50:0.173 ± 0.04 μg/mL), both extracts demonstrated dose‐dependent, significant (p < 0.01/p < 0.05) inhibition of the enzyme. FPPB increased cerebral Na+/K+ATPase activity but neither phenolic extract affects cerebral AChE/BuChE activities. HPLC‐DAD revealed catechin, caffeic acid, and quercetin, respectively, as the major phenolics (mg/g) in FPPB (29.85, 30.29, and 17.10) and BPPB (32.70, 30.51, and 19.25). Conclusion The effects of P biglobosa on ACE and cerebral ATPase are related to its constituent phenolics. ACE inhibition could be an important mechanism underlying the documented hypotensive effect of the plant. Phenolic fingerprinting, antioxidant activities and effects of free phenols (FPPB) and bound phenols (BPPB) of Parkia biglobosa leaves on some neuro‐cardiovascular enzymes were evaluated. On the overall, FPPB showed better antioxidant activity than BPPB and compared well with reference standards. FPPB also inhibits angiotensin‐1‐converting enzyme (ACE) and augments cerebral Na+/K+ ATPase. The effects of P. biglobosa on the enzymes are thus related to its constituent phenols and the documented hypotensive effect of the plant could proceed via ACE inhibition mechanism.