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Angiotensin (1-7)
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Vilon
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About Angiotensin (1-7)
Binds Mas receptor (MasR), activating nitric oxide synthase and reducing oxidative stress. Opposes TGF-β and angiotensin II signaling to reduce fibrosis. Enhances insulin sensitivity and provides cardiovascular protection.
Angiotensin-(1-7) [Ang-(1-7)] is an endogenous heptapeptide hormone generated primarily through cleavage of angiotensin II by ACE2, functioning as a counter-regulatory arm of the renin-angiotensin system (RAS) by binding the Mas receptor to promote vasodilation, anti-fibrotic, anti-inflammatory, and cardioprotective effects that oppose the vasoconstrictive actions of angiotensin II. Ang-(1-7) acts through the ACE2/Mas receptor axis to reduce oxidative stress, attenuate NF-kB-mediated inflammation, and suppress TGF-beta fibrosis signaling; the ACE2/Ang-(1-7)/Mas axis has emerged as a key regulatory pathway in cardiovascular and metabolic disease, and gained renewed research attention given ACE2's role as the SARS-CoV-2 entry receptor. A Phase 1-2 randomized clinical trial of Ang-(1-7) infusion in COVID-19 ICU patients reported preliminary safety, tolerability, and dose-response data, providing the primary indexed human pharmacokinetic evidence; broader cardiovascular protective applications are supported by preclinical data but have not been established by completed Phase 3 trials. Ang-(1-7) has no FDA approval and no approved therapeutic indication in any jurisdiction; it is an endogenous peptide under active clinical investigation as a candidate for cardiovascular, metabolic, and inflammatory conditions, with emerging human safety data but an incomplete evidence base for any specific approved clinical use.
Research Areas
About Vilon
Synthetic dipeptide Lys-Glu; modulates T-cell and NK cell activity; reduces age-related immune decline; normalizes cytokine production via epigenetic gene regulation
Vilon is a synthetic dipeptide (Lys-Glu, KE) classified as a Khavinson-class bioregulator originally derived from thymic tissue, proposed to modulate immune function in aging subjects by providing minimal thymic regulatory dipeptide signals that support T-lymphocyte activation and immune homeostasis diminished by age-related thymic involution. As the minimal active dipeptide unit of the Khavinson thymic bioregulator class, vilon is proposed to act through amino acid transporter uptake and modulation of intracellular signaling — including sphingomyelin pathway signal transduction in thymocytes — to restore T-cell activation thresholds and proliferative responses in immune cells from elderly subjects. Research has characterized natural and synthetic thymic peptides including vilon as therapeutic candidates for immune dysfunction, and experimental work has demonstrated that short Khavinson-class peptides modulate thymocyte blast transformation and sphingomyelin pathway signaling in immune cell preparations. Vilon has no FDA approval; evidence derives from Khavinson-series Russian preclinical and observational studies, and it has no regulatory approval in any major Western jurisdiction.
Research Areas
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Angiotensin (1-7)
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Vilon
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