Bradykinin (1-7) is an amino-truncated Bradykinin peptide. Bradykinin (1-7) is a metabolite of Bradykinin, cleaved by endopeptidase.
CAT No: 10-101-291
CAS No:23815-87-4
Synonyms/Alias:23815-87-4;BRADYKININ (1-7);Arg-Pro-Pro-Gly-Phe-Ser-Pro;bradykinin 1-7;H-Arg-Pro-PRO-Gly-Phe-Ser-Pro-OH;Des-8,9-BK;8-Des-phe-9-des-arg-BK;Des-phe(8)-arg(9)-BK;(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-1-[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carboxylic acid;[des-Phe(8), des-Arg(9)]-bradykinin;1-7-Bradykinin;RPPGFSP;bradykinin-(1-7);Bradykinin, des-phe(8)-des-arg(9)-;des-Phe8-Arg9-BK;R-P-P-G-F-S-P;8-De-phe-9-de-arg-bradykinin;Bradykinin (1-7) acetate salt;DTXSID30946609;CHEBI:149658;HY-P1484;BK 1-7;AKOS030622986;AS-57945;FB108563;CS-0044423;L-Arg-L-Pro-L-Pro-Gly-L-Phe-L-Ser-L-Pro;des-phenylalanyl(8)-des-arginine(9)-bradykinin;G12212;Bradykinin, des-phenylalanyl(8)-des-arginine(9)-;H-Arg-Pro-Pro-Gly-Phe-Ser-Pro-OH; H-RPPGFSP-OH;Bradykinin, 8-de(L-phenylalanine)-9-de-L-arginine-;L-arginyl-L-prolyl-L-prolylglycyl-L-phenylalanyl-L-seryl-L-proline;(S)-1-((S)-2-((S)-2-(2-((S)-1-((S)-1-((S)-2-amino-5-guanidinopentanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carboxamido)acetamido)-3-phenylpropanamido)-3-hydroxypropanoyl)pyrrolidine-2-carboxylic acid;N-(2-{[2-({[1-(Arginylprolyl)pyrrolidin-2-yl](hydroxy)methylidene}amino)-1-hydroxyethylidene]amino}-1-hydroxy-3-phenylpropylidene)serylproline;
Chemical Name:(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-1-[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carboxylic acid
Bradykinin 1-7, a heptapeptide fragment derived from the enzymatic cleavage of bradykinin, represents a valuable tool in the study of peptide signaling and vascular biology. Characterized by its unique sequence and bioactivity, Bradykinin 1-7 has garnered attention for its distinct physiological roles separate from those of the parent molecule. Its shorter chain structure retains certain biological activities while displaying altered receptor affinities, making it an intriguing subject for researchers examining the intricacies of the kallikrein-kinin system. As a research reagent, this peptide fragment enables the exploration of specific pathways and mechanisms that are modulated by bradykinin derivatives, thus advancing the understanding of peptide-mediated cellular responses in various biological systems.
Vascular Biology Research: Bradykinin 1-7 is widely employed in vascular biology studies to elucidate the mechanisms underlying vasodilation and endothelial function. By applying this peptide fragment to isolated vessel preparations or cultured endothelial cells, researchers can investigate its impact on nitric oxide production, endothelial permeability, and smooth muscle relaxation. These experiments are instrumental in distinguishing the specific contributions of bradykinin metabolites to vascular tone regulation and the modulation of blood flow, providing insights that are crucial for cardiovascular research and the development of novel therapeutic strategies targeting vascular disorders.
Inflammation and Immune Modulation: In the context of inflammation, Bradykinin 1-7 serves as a valuable probe for dissecting the roles of kinin fragments in immune cell signaling and inflammatory mediator release. Experimental models utilizing this peptide allow scientists to observe its effects on leukocyte migration, cytokine secretion, and the activation of intracellular signaling cascades. Such studies help clarify how bradykinin derivatives contribute to the initiation and resolution of inflammatory responses, as well as their potential interactions with other peptide mediators in the immune system.
Receptor Pharmacology: The distinct receptor binding profile of Bradykinin 1-7 makes it an essential tool for receptor pharmacology investigations. Researchers utilize this fragment to characterize the selectivity and affinity of bradykinin receptors, particularly when differentiating between B1 and B2 receptor subtypes. Through binding assays and functional studies, the peptide aids in mapping receptor-ligand interactions, elucidating downstream signaling pathways, and identifying potential allosteric modulators. These findings are critical for the rational design of receptor-targeted compounds and for understanding the nuanced roles of kinin fragments in cellular communication.
Peptide Metabolism Studies: Metabolic stability and enzymatic processing of kinins are central to understanding their physiological and pathophysiological functions. Bradykinin 1-7 is frequently utilized in studies examining the activity of kininases and other proteolytic enzymes involved in kinin metabolism. By tracking the generation and degradation of this fragment in biological samples, researchers can assess enzyme specificity, kinetic parameters, and the influence of various inhibitors. Such work sheds light on the metabolic fate of kinins in vivo and informs the development of enzyme-targeted interventions.
Neurobiology and Sensory Research: The role of bradykinin fragments in the nervous system is an emerging area of investigation, with Bradykinin 1-7 being used to explore its effects on neuronal signaling and sensory perception. Studies involving this peptide assess its ability to modulate neurotransmitter release, influence pain pathways, and interact with sensory receptors. These investigations contribute to a deeper understanding of how kinin fragments participate in neural communication and sensory processing, potentially revealing new avenues for research in neurobiology and pain management.
Signal Transduction Analysis: As a model peptide, Bradykinin 1-7 is instrumental in the dissection of intracellular signaling events triggered by kinin receptor activation. Through the use of advanced biochemical and imaging techniques, scientists employ this fragment to monitor changes in second messenger levels, protein phosphorylation states, and gene expression profiles. Such analyses provide a detailed map of the molecular events downstream of kinin receptor engagement, facilitating the identification of novel regulatory nodes and potential drug targets within the kinin signaling network.
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