Bradykinin (1-6) is an amino-truncated Bradykinin peptide. Bradykinin (1-6) is a stable metabolite of Bradykinin, cleaved by carboxypeptidase Y (CPY).
CAT No: R1248
CAS No:23815-88-5
Synonyms/Alias:Bradykinin (1-6);23815-88-5;(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-hydroxypropanoic acid;Arg-Pro-Pro-Gly-Phe-Ser;SCHEMBL9796839;Bradykinin (1-6) acetate salt;HY-P1469;FB108561;MS-31010;CS-0044401;G12211;H-Arg-Pro-Pro-Gly-Phe-Ser-OH; H-RPPGFS-OH;Argininyl-prolinyl-prolinyl-glycinyl-phenylalaninyl-serine;(S)-2-((S)-2-(2-((S)-1-((S)-1-((S)-2-amino-5-guanidinopentanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carboxamido)acetamido)-3-phenylpropanamido)-3-hydroxypropanoic acid;
Bradykinin 1-6 is a peptide fragment derived from the N-terminal region of the nonapeptide bradykinin, a well-characterized vasoactive mediator in mammalian systems. As a hexapeptide, Bradykinin 1-6 retains the initial sequence of the parent molecule, allowing researchers to investigate the functional contributions of this segment to the overall biological activity of bradykinin. The structural and sequence specificity of this peptide fragment makes it a valuable tool for dissecting receptor interactions, enzymatic processing, and signaling mechanisms associated with kinins. Its defined sequence and biochemical properties have established its relevance in studies of peptide-receptor binding, proteolytic degradation pathways, and the development of peptide-based probes for physiological and pharmacological research.
Peptide-receptor interaction studies: Bradykinin 1-6 is frequently employed to elucidate the binding preferences and activation profiles of bradykinin receptors, particularly B1 and B2 subtypes. Researchers utilize this hexapeptide to map minimal recognition motifs required for receptor activation or inhibition, providing insight into the structural determinants that govern ligand specificity. By comparing the bioactivity of the fragment with that of the full-length peptide, studies can distinguish the contributions of the N-terminal residues to receptor affinity and downstream signaling, facilitating the design of selective agonists or antagonists for kinin receptor research.
Enzymatic degradation and metabolic pathway analysis: The hexapeptide serves as a model substrate for investigating the proteolytic enzymes responsible for bradykinin inactivation, such as angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), and aminopeptidases. By monitoring the enzymatic cleavage of Bradykinin 1-6, scientists can characterize the specificity, kinetics, and regulatory mechanisms of these peptidases in vitro. This application aids in mapping the metabolic fate of bradykinin fragments in biological fluids and tissues, enhancing understanding of kinin turnover and homeostasis in physiological and pathophysiological contexts.
Structure-activity relationship (SAR) studies: The well-defined sequence of Bradykinin 1-6 makes it an ideal candidate for SAR investigations aimed at correlating specific amino acid residues or sequence motifs with biological function. Through systematic substitution, truncation, or modification of individual residues within the hexapeptide, researchers can assess the impact on receptor binding, enzymatic stability, or biological activity. These studies are instrumental in guiding the rational design of peptide analogs with tailored properties for use as research probes or lead compounds in drug discovery programs targeting the kinin system.
Development of analytical standards and assay controls: Due to its defined molecular structure and sequence, Bradykinin 1-6 is widely used as a reference standard or control material in analytical assays, including high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its inclusion enables accurate calibration, method validation, and quantification of peptide fragments in complex biological samples. The fragment's stability and reproducibility make it suitable for standardizing experimental protocols and ensuring the reliability of peptide detection and measurement in research laboratories.
Peptide synthesis and modification research: Bradykinin 1-6 also serves as a model substrate for evaluating peptide synthesis methodologies and post-synthetic modifications. Its relatively short sequence allows for efficient solid-phase synthesis, facilitating the optimization of coupling strategies, protecting group schemes, and purification techniques. Furthermore, the hexapeptide provides a platform for introducing site-specific modifications, such as labeling with fluorescent tags or isotopic markers, which are valuable for developing advanced analytical tools and imaging probes in peptide research.
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