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 is a peptide fragment derived from the N-terminal sequence of bradykinin, a well-known nonapeptide involved in the kallikrein-kinin system. As a heptapeptide, Bradykinin 1-7 retains a portion of the biological activity associated with its parent molecule, yet displays distinct pharmacological and biochemical properties. Its structural features make it an important tool for dissecting the functional domains of bradykinin and understanding the structure-activity relationships that govern peptide-mediated signaling. Researchers utilize this fragment to probe the mechanisms of kinin receptor activation, peptide metabolism, and the broader physiological roles of kinins in inflammation, vascular biology, and pain pathways.
Receptor binding studies: Bradykinin 1-7 is frequently used in receptor binding assays to elucidate the specificity and affinity of bradykinin receptor subtypes, particularly B1 and B2 receptors. By comparing its binding characteristics to those of full-length bradykinin and other fragments, investigators can determine which peptide domains are critical for receptor interaction and activation. This approach helps clarify the molecular determinants of ligand-receptor recognition and supports the rational design of peptide analogs with tailored pharmacological profiles.
Peptide metabolism research: The heptapeptide serves as a valuable substrate for investigating the enzymatic pathways responsible for bradykinin degradation. By tracking the generation and subsequent breakdown of Bradykinin 1-7 in biological samples, scientists gain insight into the activity of kininases and related peptidases. These studies are essential for mapping the metabolic fate of kinins, understanding their physiological half-life, and identifying potential regulatory checkpoints in kinin-mediated signaling cascades.
Inflammatory pathway modeling: In experimental models of inflammation, Bradykinin 1-7 is utilized to dissect the contributions of specific peptide fragments to the modulation of vascular permeability, edema formation, and leukocyte recruitment. Its use enables researchers to differentiate between the effects mediated by intact bradykinin and those attributable to its metabolites. This distinction is crucial for unraveling the complex interplay between peptide structure and pro-inflammatory activity, informing the development of new anti-inflammatory strategies.
Signal transduction analysis: The fragment is also employed in studies focused on intracellular signaling events triggered by kinin receptor activation. By applying Bradykinin 1-7 to cultured cells or tissue preparations, investigators can monitor downstream responses such as calcium mobilization, kinase activation, and gene expression changes. These experiments help delineate the signaling pathways selectively engaged by different bradykinin fragments and provide a mechanistic framework for interpreting the physiological outcomes of kinin system modulation.
Peptide structure-function investigations: Bradykinin 1-7 is instrumental in systematic structure-activity relationship (SAR) studies aimed at pinpointing the minimal peptide sequence required for specific biological effects. Through comparative analyses with other bradykinin-derived peptides, researchers can identify the amino acid residues essential for activity and explore the influence of sequence modifications on potency and selectivity. Such knowledge is pivotal in guiding the design of novel peptide probes and therapeutic leads targeting the kinin system.
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