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Related Concept Videos

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors01:30

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Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
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Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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The activation of the sympathetic nervous system and the renin-angiotensin-aldosterone system (RAAS) contributes to cardiac remodeling, and inhibiting the RAAS is a pharmacological target in heart failure management. As a result, neurohumoral modulation is a crucial treatment principle for managing heart failure. This approach involves using medications like ACE inhibitors (ACEIs), angiotensin receptor blockers (ARBs), β-blockers, mineralocorticoid receptor antagonists (MRAs), and neutral...
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The renin-angiotensin-aldosterone system (RAAS) is an intricate physiological pathway involving numerous enzymes and hormones, including renin, angiotensin-converting enzyme (ACE), angiotensin I and II, and aldosterone. Imbalances within this system increase the production of angiotensin II and aldosterone. Increased angiotensin II levels promote vasoconstriction and blood pressure elevation. Concurrently, higher aldosterone levels stimulate sodium and water reabsorption in the kidneys,...
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In the renin-angiotensin-aldosterone system, a hormone called angiotensin II plays a crucial role. It binds to the AT1 receptors in vascular smooth muscles coupled with Gq proteins. The activation of these receptors activates an enzyme called phospholipase C, which releases two molecules: inositol trisphosphate and diacylglycerol. These molecules cause a chain reaction that leads to the phosphorylation of myosin light chains and promotes interaction between actin and myosin, leading to smooth...
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Endothelins (ETs) are potent vasoactive peptides critical in the human body's various physiological and pathological processes. One of the most promising therapeutic strategies for treating pulmonary arterial hypertension (PAH) involves counteracting the effects of these endothelins using a class of drugs known as endothelin receptor antagonists.
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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.

ACS Medicinal Chemistry Letters
|December 17, 2025
PubMed
Summary

Two novel bioactive peptides show potential for controlling hypertension by inhibiting angiotensin-converting enzyme (ACE). These peptides may lead to new antihypertensive drugs with fewer side effects.

Keywords:
Angiotensin-Converting EnzymeAntihypertensiveBioactive PeptidesHypertensionMolecular Docking

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Cardiovascular Research

Background:

  • Hypertension is a leading global cause of mortality, often poorly managed due to adverse effects of current treatments.
  • The renin-angiotensin system (RAS) and its key enzyme, angiotensin-converting enzyme (ACE), are critical targets for antihypertensive therapies.
  • Bioactive peptides are recognized for their diverse biological activities, including potential antihypertensive properties.

Purpose of the Study:

  • To identify and characterize novel bioactive peptides with angiotensin-converting enzyme (ACE) inhibitory activity.
  • To evaluate the potential of these peptides as a basis for developing new antihypertensive drugs.

Main Methods:

  • Synthesis and characterization of two novel peptides: MSFLEHFLELK (PepDB_AHP1) and VWTNCYHLYPAH (PepDB_AHP4).
  • In vitro assessment of peptide interaction with the active site of angiotensin-converting enzyme (ACE).
  • Determination of inhibitory concentrations (IC50) for the identified peptides against ACE.

Main Results:

  • Both novel peptides, PepDB_AHP1 and PepDB_AHP4, demonstrated interaction with key residues in the ACE active site.
  • The IC50 values for PepDB_AHP1 and PepDB_AHP4 were determined to be 331.2 μM and 88.63 μM, respectively.
  • These findings indicate significant ACE inhibitory potential for both peptides.

Conclusions:

  • The novel peptides PepDB_AHP1 and PepDB_AHP4 exhibit promising angiotensin-converting enzyme (ACE) inhibitory activity.
  • These peptides can serve as valuable models for the future development of optimized ACE inhibitors.
  • Further research into these peptides could lead to novel therapeutic strategies for hypertension management.