Efficacy of a Novel ACE-Inhibitory Peptide from <i>Sargassum Maclurei</i> in Hypertension and Reduction of Intracellular Endothelin-1

• Main Authors: Yajun Zheng, Yufeng Zhang, Sang San
• Format: Article
• Language: English
• Published: MDPI AG 2020-02-01
• Series: Nutrients
• Subjects: sargassum maclurei protein; angiotensin i-converting enzyme; in silico analysis; inhibition kinetics; molecular docking; spontaneously hypertensive rats; endothelin-1
• Online Access: https://www.mdpi.com/2072-6643/12/3/653

Sargassum maclurei is a potential protein resource because of its high protein content and relatively balanced amino acid composition. To promote its usage in food, medical, or other industries, S. maclurei protein was hydrolyzed by pepsin and papain to obtain bioactive peptides. The S. maclurei protein hydrolysates (SMPHs) were purified using gel chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), and 12 major fractions were obtained. The fraction D11 with the highest angiotensin I-converting enzyme (ACE) inhibition (61.59%, at 1 mg/ mL) was subjected to liquid chromatography-mass spectrometry (LC-MS/MS) analysis, and about 17 peptides were identified, of which the RWDISQPY (1063.5 Da) was chosen to be synthesized based on in silico analysis. The RWDISQPY demonstrated high ACE inhibition ability (IC₅₀: 72.24 &#956;M) with competitive inhibition mode, and could effectively (<i>p </i>&lt; 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 150 mg/kg body weight. The results of the molecular docking simulation demonstrated that RWDISQPY could bind with the active sites S1 and S2 of ACE via short hydrogen bonds. Moreover, RWDISQPY showed acceptable endothelin-1 suppressing capacity (26.21% at 1.5 mg/mL). These results indicate that S. maclurei could be developed into functional foods such as antihypertensive products.