Characterization of Novel Angiotensin-Converting Enzyme Inhibitory Peptides
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. IC<sub>50</sub> 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.
Authors
- Lucélia Santi (ORCID: https://orcid.org/0000-0002-5698-7006)
- Emerson G. Moreira (ORCID: https://orcid.org/0000-0001-7887-7601)
- Walter O. Beys‐da‐Silva (ORCID: https://orcid.org/0000-0001-8329-7839)
- Camila Innocente-Alves (ORCID: https://orcid.org/0000-0002-1264-4888)
- Hugo Verli (ORCID: https://orcid.org/0000-0002-4796-8620)
- Raul Izidoro Carneiro
- Sara Luísa Sulzbach (ORCID: https://orcid.org/0000-0002-5476-0174)
Institutions
- Universidade Federal do Rio Grande do Sul (BR)
- Deoxi Biotecnologia (Brazil) (BR)
- Sociedade Brasileira de Biologia Celular (BR)
Publication Details
- Journal
- ACS Medicinal Chemistry Letters
- Published
- 2025-11-26
- DOI
- https://doi.org/10.1021/acsmedchemlett.5c00569
- Primary Topic
- Protein Hydrolysis and Bioactive Peptides
- Type
- article
- Field-Weighted Citation Impact
- 0.00