ArticleFEBS letters2024
Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP.
Article in FEBS letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- Marine-Derived Proteins: Individual Variability in Health Effects Across Protein Structure, Host Genetics, and Gut Microbiota.Comprehensive reviews in food science and food safety · 2026Review
- The Role of Rho-associated Kinase in the Cognitive Benefits of the ACE Inhibitory Peptide LAP for Hypertension.Current molecular medicine · 2026Article
- Molecular Basis of Dipeptide Recognition inBiomolecules · 2025Article
- Uncovering the Potential Somatic Angiotensin-Converting Enzyme (sACE) Inhibitory Capacity of Peptides fromFoods (Basel, Switzerland) · 2024Article
- Ile-Pro-Pro attenuates sympathetic activity and hypertension.Journal of physiology and biochemistry · 2024Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Human somatic angiotensin-1-converting enzyme (sACE) is composed of a catalytic N-(nACE) and C-domain (cACE) of similar size with different substrate specificities. It is involved in the regulation of blood pressure by converting angiotensin I to the vasoconstrictor angiotensin II and has been a major focus in the development of therapeutics for hypertension. Bioactive peptides from various sources, including milk, have been identified as natural ACE inhibitors. We report the structural basis for the role of two lacototripeptides, Val-Pro-Pro and Ile-Pro-Pro, in domain-specific inhibition of ACE using X-ray crystallography and kinetic analysis. The lactotripeptides have preference for nACE due to altered polar interactions distal to the catalytic zinc ion. Elucidating the mechanism of binding and domain selectivity of these peptides also provides important insights into the functional roles of ACE.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.