Bradykinin (1-5) is a major stable metabolite of Bradykinin, formed by the proteolytic action of angiotensin-converting enzyme (ACE).
CAT No: R1247
CAS No:23815-89-6
Synonyms/Alias:Bradykinin (1-5);23815-89-6;Arg-pro-pro-gly-phe;Thrombostatin;H-Arg-Pro-PRO-Gly-Phe-OH;Arginyl-prolyl-prolyl-glycyl-phenylalanine;H-ARG-PRO-PRO-GLY-PHE-OH TRIFLUOROACETATE SALT;CHEMBL1927653;L-Phenylalanine, N-(N-(1-(1-L-arginyl-L-prolyl)-L-prolyl)glycyl)-;L-arginyl-L-prolyl-L-prolylglycyl-L-phenylalanine;(2S)-2-[[2-[[(2S)-1-[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-phenylpropanoic acid;Bradykinin (1-5) trifluoroacetate salt;1-5-Bradykinin(9ci);Arg1-Pro2-Pro3-Gly4-Phe5;SCHEMBL8072324;DTXSID40946610;USSUMSBPLJWFSZ-TUFLPTIASA-N;HY-P1488;BDBM50359564;AKOS030622985;AS-66956;FB108560;H-Arg-Pro-Pro-Gly-Phe-OH; H-RPPGF-OH;CS-0044432;F77804;(2S)-2-(2-{[(2S)-1-[(2S)-1-[(2S)-2-AMINO-5-CARBAMIMIDAMIDOPENTANOYL]PYRROLIDINE-2-CARBONYL]PYRROLIDIN-2-YL]FORMAMIDO}ACETAMIDO)-3-PHENYLPROPANOIC ACID;(S)-2-(2-((S)-1-((S)-1-((S)-2-amino-5-guanidinopentanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carboxamido)acetamido)-3-phenylpropanoic acid;N-[2-({[1-(Arginylprolyl)pyrrolidin-2-yl](hydroxy)methylidene}amino)-1-hydroxyethylidene]phenylalanine;
Bradykinin 1-5 is a peptide fragment derived from the proteolytic cleavage of the nonapeptide bradykinin, comprising the first five amino acid residues of the parent molecule. As a bioactive pentapeptide, it represents a significant product of kinin metabolism and is recognized for its distinct biochemical properties compared to full-length bradykinin. The fragment's generation and activity are of considerable interest in the study of the kallikrein-kinin system, inflammation, and vascular biology. Its relatively short sequence confers unique stability and receptor interaction profiles, making it a valuable tool for dissecting the physiological and pathophysiological roles of kinin-derived peptides.
Peptide signaling research: Bradykinin 1-5 serves as a critical tool for elucidating the mechanisms of peptide-mediated signal transduction, particularly within the context of the kallikrein-kinin system. Researchers employ this fragment to investigate how truncated kinins interact with cellular receptors, modulate downstream signaling cascades, and influence physiological responses such as vasodilation, vascular permeability, and inflammatory processes. Its use enables the differentiation between the biological activities of full-length bradykinin and its shorter metabolites, thereby providing insight into the fine-tuning of kinin signaling pathways.
Enzymatic cleavage studies: The pentapeptide is frequently utilized as a model substrate in enzymology to characterize the activity of kininases and related proteases involved in bradykinin degradation. By monitoring the generation and further metabolism of Bradykinin 1-5, researchers can delineate the specificity, kinetics, and regulatory mechanisms of enzymes such as angiotensin-converting enzyme (ACE), neprilysin, and aminopeptidases. These studies are fundamental for understanding the regulation of peptide bioavailability and the physiological termination of kinin-mediated signals.
Receptor specificity assays: Bradykinin 1-5 provides a valuable tool for studying the binding affinity and activation profiles of bradykinin receptors, especially B1 and B2 subtypes. As a truncated fragment, it allows for the assessment of receptor selectivity and partial agonism or antagonism, thereby aiding in the mapping of functional domains critical for receptor interaction. Such assays are essential for the rational design of receptor modulators and for advancing pharmacological research targeting the kinin system.
Inflammation and vascular biology models: The peptide fragment is employed in experimental models to investigate its effects on endothelial function, vascular tone, and inflammatory mediator release. Its application enables the assessment of kinin fragment activity in modulating leukocyte trafficking, cytokine production, and microvascular dynamics. These studies contribute to a more nuanced understanding of the role of kinin metabolites in both acute and chronic inflammatory states, as well as in the regulation of blood pressure and tissue perfusion.
Peptide metabolism analysis: Bradykinin 1-5 is widely used as a reference compound in analytical chemistry and mass spectrometry to validate methods for detecting kinin fragments in biological samples. Its defined sequence and known fragmentation pattern make it an ideal standard for optimizing chromatographic separation, quantitation, and identification protocols in bioanalytical workflows. This application supports research into endogenous peptide turnover, biomarker discovery, and the pharmacokinetics of kinin-derived peptides in various experimental systems.
1. Emu oil in combination with other active ingredients for treating skin imperfections
2. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry
4. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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