Bradykinin, des-pro(3)- incorporates a targeted modification that alters structural flexibility and binding preferences. Removal of proline influences turn formation and backbone geometry. Researchers examine its solvent-dependent conformations and interaction profiles. Uses include motif-function studies, structure-activity exploration, and peptide analog design.
CAT No: R2671
CAS No:80943-05-1
Synonyms/Alias:Arg-pro-gly-phe-ser-pro-phe-arg;80943-05-1;3-De-pro-bradykinin;Bradykinin, des-pro(3)-;Bradykinin, des-proline(3)-;Bradykinin, 3-de-L-proline-;[Des-Pro2]-Bradykinin;(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid;HY-P2828;CS-0143033;H-L-Arg-L-Pro-Gly-L-Phe-L-Ser-L-Pro-L-Phe-L-Arg-OH;(2S)-2-[(2S)-2-{[(2S)-1-[(2S)-2-[(2S)-2-(2-{[(2S)-1-[(2S)-2-AMINO-5-CARBAMIMIDAMIDOPENTANOYL]PYRROLIDIN-2-YL]FORMAMIDO}ACETAMIDO)-3-PHENYLPROPANAMIDO]-3-HYDROXYPROPANOYL]PYRROLIDIN-2-YL]FORMAMIDO}-3-PHENYLPROPANAMIDO]-5-CARBAMIMIDAMIDOPENTANOIC ACID;(S)-2-((S)-2-((S)-1-((S)-2-((S)-2-(2-((S)-1-((S)-2-Amino-5-guanidinopentanoyl)pyrrolidine-2-carboxamido)acetamido)-3-phenylpropanamido)-3-hydroxypropanoyl)pyrrolidine-2-carboxamido)-3-phenylpropanamido)-5-guanidinopentanoic acid;
Bradykinin, des-pro(3)- is a specialized peptide derivative that has garnered considerable attention within the biochemical and pharmacological research communities. Characterized by the removal of the proline residue at position three, this modified bradykinin analog exhibits unique structural and functional properties compared to its parent molecule. Its distinct configuration enables researchers to investigate the nuances of bradykinin receptor interactions, enzymatic degradation pathways, and signal transduction mechanisms. The versatility of Bradykinin, des-pro(3)- makes it an invaluable tool in the exploration of peptide-mediated physiological responses, particularly those involving the kallikrein-kinin system. As a research-grade compound, it is frequently utilized in experimental settings that demand high specificity and sensitivity in the modulation of vascular and inflammatory processes.
Receptor Binding Studies: Bradykinin, des-pro(3)- serves as a powerful probe for dissecting the binding characteristics of bradykinin receptors, particularly B1 and B2 subtypes. By examining the affinity and selectivity of this analog in comparison to native bradykinin, scientists can elucidate the structural determinants that govern receptor activation and downstream signaling. Such studies are pivotal for mapping ligand-receptor interactions and for designing novel receptor modulators with therapeutic potential. The use of this peptide in competitive binding assays and receptor-ligand modeling enhances our understanding of peptide-receptor specificity and the molecular basis of signal transduction within the kinin system.
Enzymatic Degradation Research: The unique structure of des-pro(3)-bradykinin renders it an excellent substrate for investigating the activity of kininases and other peptidases involved in bradykinin metabolism. Researchers employ this analog to monitor the cleavage patterns and degradation kinetics mediated by enzymes such as angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP). These studies are instrumental in identifying enzyme specificity, inhibitor efficacy, and the metabolic fate of kinins under physiological and pathological conditions. By leveraging this compound, scientists can dissect the enzymatic pathways that regulate peptide bioavailability and duration of action.
Inflammatory Pathway Analysis: As an analog of bradykinin, des-pro(3)-bradykinin is utilized to probe the molecular and cellular mechanisms underlying inflammatory responses. Its application in in vitro and ex vivo models allows for the assessment of its capacity to induce or modulate the release of pro-inflammatory mediators, such as cytokines and prostaglandins. This research direction provides valuable insights into the contribution of the kallikrein-kinin system to inflammation, edema, and pain, facilitating the identification of novel anti-inflammatory targets and strategies.
Vascular Permeability Investigations: The ability of bradykinin analogs to modulate endothelial barrier function is well-documented, and des-pro(3)-bradykinin is no exception. Researchers employ this peptide to study changes in vascular permeability, endothelial cell signaling, and the mechanisms governing fluid extravasation. These investigations are crucial for understanding the role of kinins in cardiovascular physiology, tissue injury, and repair processes. By using this analog, scientists can delineate the specific contributions of individual peptide fragments to vascular homeostasis.
Signal Transduction Pathway Elucidation: The application of des-pro(3)-bradykinin extends to the detailed mapping of intracellular signaling cascades triggered by kinin receptor activation. Experimental models utilizing this peptide facilitate the study of secondary messenger systems, protein phosphorylation events, and gene expression profiles that are downstream of receptor engagement. Such research is fundamental for uncovering the molecular mechanisms by which kinins influence cellular function, adaptation, and communication. Collectively, these diverse applications underscore the significance of Bradykinin, des-pro(3)- as a multifaceted tool in biochemical, pharmacological, and physiological research, fostering advancements in our understanding of peptide-mediated signaling networks and their broader implications in health and disease.
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