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Updated: Jan 8, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Characterization of Novel Angiotensin-Converting Enzyme Inhibitory Peptides
Camila Innocente-Alves1,2, Sara Luísa Sulzbach1, Emerson Gonçalves Moreira3
1Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Porto Alegre 90010-150, Brazil.
Abstract:
Hypertension is implicated in the highest number of deaths worldwide. Despite awareness of its complications and the availability of several antihypertensive treatments, hypertension remains poorly controlled, often due to adverse effects that can hinder adherence. Angiotensin-converting enzyme (ACE), a key enzyme of the renin-angiotensin system (RAS), is an important therapeutic target. Bioactive peptides have been extensively researched for their biological activities, including their antihypertensive potential. Here, we describe two novel peptides, MSFLEHFLELK (PepDB_AHP1) and VWTNCYHLYPAH (PepDB_AHP4). Both peptides interact with residues at ACE's active site, such as His353, Ala354, and Val380. IC50 values were 331.2 and 88.63 μM, respectively. These peptides may serve as models for further optimization aimed at the development of novel ACE-inhibitory drugs.
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