Key result
Two novel peptides, MSFLEHFLELK and VWTNCYHLYPAH, demonstrated angiotensin-converting enzyme inhibitory activity with IC50 values of 331.2 and 88.63 μM, respectively.
Two novel peptides demonstrate ACE inhibitory activity in vitro, providing potential models for developing new antihypertensive drugs.
May guide peptide-based ACE inhibitor development; leaves open clinical translation in hypertension.
High Resolution Image Download MS PowerPoint Slide 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 50 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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Innocente-Alves et al. (2025) studied Hypertension. Novel peptides MSFLEHFLELK (PepDB_AHP1) and VWTNCYHLYPAH (PepDB_AHP4) was evaluated on ACE inhibition (IC50). Two novel peptides, MSFLEHFLELK and VWTNCYHLYPAH, demonstrated angiotensin-converting enzyme inhibitory activity with IC50 values of 331.2 and 88.63 μM, respectively.