Bradykinin is an active peptide that is generated by the kallikrein-kinin system. It is a inflammatory mediator and also recognized as a neuromediator and regulator of several vascular and renal functions.
CAT No: R1245
CAS No:58-82-2
Chemical Name:(2S)-2-[[(2S)-2-[[(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-carbonyl]amino]-3-phenylpropanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
Bradykinin is a naturally occurring nonapeptide that plays a pivotal role in various physiological and pathophysiological processes, particularly within the kallikrein-kinin system. As a potent vasoactive peptide, it is renowned for its ability to induce vasodilation, increase vascular permeability, and mediate pain and inflammatory responses. Its significance extends to cardiovascular, renal, and inflammatory research, where it serves as a critical tool for elucidating peptide signaling pathways and receptor-mediated mechanisms. The unique biochemical properties and receptor specificity of bradykinin have made it an indispensable reagent in peptide research and functional studies.
Receptor Pharmacology: Bradykinin is widely employed in receptor pharmacology to study the activation and signaling of B1 and B2 kinin receptors. By serving as a selective agonist, it allows researchers to investigate receptor-ligand interactions, downstream signaling cascades, and the physiological consequences of receptor modulation. These studies provide valuable insights into the molecular mechanisms underlying vascular tone regulation, inflammation, and pain perception, supporting the development of novel receptor-targeted compounds for research applications.
Vascular Biology Research: The peptide is a key experimental tool in vascular biology, particularly for exploring mechanisms of endothelium-dependent vasodilation and vascular permeability. Its application enables the dissection of nitric oxide and prostaglandin-mediated pathways, as well as the study of endothelial barrier function. Utilizing bradykinin in in vitro and ex vivo models helps elucidate the cellular and molecular events that govern microvascular responses, contributing to a deeper understanding of cardiovascular physiology and pathophysiology.
Inflammation and Pain Mechanisms: Bradykinin's role as a mediator of acute and chronic inflammation makes it highly valuable for studying the molecular basis of inflammatory and nociceptive pathways. Researchers use it to induce and analyze inflammatory responses in cellular and tissue models, facilitating the identification of key mediators, signaling molecules, and regulatory mechanisms involved in pain sensitization and immune cell recruitment. Such studies are essential for advancing knowledge of inflammatory diseases and pain syndromes at the molecular level.
Peptide Functional Studies: As a model peptide, bradykinin is frequently utilized in functional assays to investigate peptide stability, metabolism, and degradation by peptidases such as angiotensin-converting enzyme (ACE) and neutral endopeptidase. These applications are critical for understanding the kinetics of peptide turnover, the specificity of enzymatic cleavage, and the regulation of bioactive peptide levels in biological systems. The use of bradykinin in these studies supports the development of enzyme inhibitors and the characterization of metabolic pathways relevant to peptide biology.
Analytical Method Development: The well-characterized structure and bioactivity of bradykinin make it a preferred standard in the development and validation of analytical methods, including mass spectrometry, high-performance liquid chromatography, and immunoassays. Its application as a reference peptide enables precise quantification, assay calibration, and method optimization in both qualitative and quantitative analyses. This facilitates accurate detection and measurement of peptides in complex biological samples, enhancing the reliability of analytical workflows in biochemical research.
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