Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from...

Area of Science:

• Biochemistry
• Marine Biotechnology
• Pharmacology

Background:

• Hypertension is a global health concern.
• Angiotensin-I-converting enzyme (ACE) plays a crucial role in blood pressure regulation.
• Oysters are a source of bioactive compounds, including selenium.

Purpose of the Study:

• To identify and characterize novel antihypertensive peptides from selenium-enriched oyster proteins.
• To evaluate the ACE inhibitory activity and cellular effects of these peptides.

Main Methods:

• Hydrolysis of selenium-enriched oyster proteins using trypsin.
• Purification of peptides using ultrafiltration and RP-HPLC.
• Identification of peptide sequences using LC-MS/MS and molecular docking.
• In vitro cellular assays to assess nitric oxide (NO) release and Endothelin-1 (ET-1) secretion.

Main Results:

• Two novel selenium-containing peptides, SeMFRTSSK and QASeMNEATGGK, were identified with high ACE inhibitory activity.
• Molecular docking confirmed strong binding affinities of these peptides to the ACE active site.
• Cellular assays showed that these peptides enhanced NO release and suppressed ET-1 secretion in EA.hy926 cells.
• The antihypertensive effects of these peptides were superior to the positive control, captopril.

Conclusions:

• Selenium-enriched oyster-derived peptides exhibit significant antihypertensive potential.
• These peptides represent promising natural ingredients for functional foods and pharmaceutical applications targeting hypertension.