Angiotensin I/II 1-5 is a peptide that contains the amino acids 1-5, which is converted from Angiotensin I/II. Angiotensin I is formed by the action of renin on angiotensinogen. Angiotensin II is produced from angiotensin I. Angiotensin II has been investigated for the treatment, basic science, and diagnostic of Hypertension, Renin Angiotensin System, and Idiopathic Membranous Nephropathy.
CAT No: R1198
CAS No:58442-64-1
Synonyms/Alias:Angiotensin (1-5);58442-64-1;Angiotensin I/II (1-5);Angiotensin I/II 1-5;(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoic acid;MFCD00214588;Angiotensin i/ii(1-5);HY-P1839;AKOS040764031;FA108792;TS-10398;H-Asp-Arg-Val-Tyr-Ile-OH; H-DRVYI-OH;CS-0096565;Q58310855;Angiotensin I/II (1-5) (H-L-Asp-L-Arg-L-Val-L-Tyr-L-Ile-OH);
Angiotensin I/II 1-5 is a bioactive peptide fragment derived from the N-terminal sequence of angiotensin I and angiotensin II, consisting of the first five amino acids. As a naturally occurring pentapeptide, it plays a significant role in the renin-angiotensin system (RAS), a critical hormonal cascade involved in the regulation of blood pressure, fluid balance, and vascular function. The compound's unique sequence and biological origin make it a valuable tool for researchers investigating the enzymatic processing, receptor interactions, and signaling pathways associated with angiotensin peptides and their metabolites. Its importance extends to studies of peptide metabolism, cardiovascular physiology, and the broader field of peptide-based regulatory mechanisms.
Peptide metabolism research: Angiotensin I/II 1-5 serves as a key substrate and product in studies focused on the enzymatic cleavage of larger angiotensin peptides by various proteases, such as angiotensin-converting enzyme (ACE) and aminopeptidases. By incorporating this pentapeptide into in vitro assays or biochemical models, researchers can dissect the specific pathways and kinetics of peptide degradation, facilitating a deeper understanding of RAS regulation and the generation of bioactive peptide fragments in physiological and pathophysiological contexts.
Receptor interaction analysis: The pentapeptide is frequently utilized in investigations aimed at elucidating the binding affinities and selectivity of angiotensin-derived fragments for cellular receptors, particularly those distinct from the classical angiotensin II type 1 and type 2 receptors. Through competitive binding assays and receptor profiling, scientists can determine whether Angiotensin I/II 1-5 modulates signaling events or acts as a regulatory ligand, thus contributing to the mapping of non-canonical pathways within the renin-angiotensin system.
Peptide signaling studies: Researchers employ this fragment to probe the downstream signaling cascades initiated by angiotensin-derived peptides in various cell types, including vascular endothelial cells, smooth muscle cells, and renal tissues. By monitoring changes in intracellular messengers, kinase activation, or gene expression profiles in response to the pentapeptide, investigators can delineate its specific signaling roles and assess its capacity to modulate physiological responses distinct from those triggered by full-length angiotensin peptides.
Analytical method development: Angiotensin I/II 1-5 is widely adopted as a reference standard or analytical probe in the development and validation of mass spectrometry, high-performance liquid chromatography (HPLC), and immunoassay techniques for the detection and quantification of angiotensin peptides in biological samples. Its defined sequence and physicochemical properties enable the optimization of separation protocols, calibration curves, and assay specificity, supporting accurate measurement of peptide levels in complex matrices such as plasma, tissue extracts, or cell culture supernatants.
Peptide synthesis and modification research: The pentapeptide's concise structure and well-characterized sequence make it a valuable model for studies on solid-phase peptide synthesis, post-translational modifications, and peptide stability. Researchers can employ Angiotensin I/II 1-5 to evaluate synthetic strategies, investigate the effects of amino acid substitutions or chemical modifications, and explore approaches for enhancing peptide solubility or resistance to enzymatic degradation, thereby advancing the development of novel peptide-based research tools and analytical standards.
3. Emu oil in combination with other active ingredients for treating skin imperfections
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More