Batifiban contains a structured peptide-derived framework enriched with aromatic and basic residues that affect receptor-binding interactions. Its arrangement supports studies of steric complementarity and solvent accessibility. Researchers examine conformational states to clarify sequence-driven activity. Uses include ligand-design optimization, binding-site mapping, and biochemical mechanism studies.
CAT No: R2503
CAS No:710312-77-9
Synonyms/Alias:Batifiban;Correctin;7AKM76YKN5;UNII-7AKM76YKN5;BAT 2094;BAT-2094;710312-77-9;L-Cysteinamide, N2-(3-mercapto-1-oxopropyl)-L-arginylglycyl-L-alpha-aspartyl-L-tryptophyl-L-prolyl-, cyclic (1->6)-disulfide;L-CYSTEINAMIDE, N2-(3-MERCAPTO-1-OXOPROPYL)-L-ARGINYLGLYCYL-L-.ALPHA.-ASPARTYL-L-TRYPTOPHYL-L-PROLYL-, CYCLIC (1->6)-DISULFIDE;DTXSID701031211;DA-71298;HY-125053;CS-0088845;2-[(3S,6S,12S,20R,23S)-20-carbamoyl-12-[3-(diaminomethylideneamino)propyl]-3-(1H-indol-3-ylmethyl)-2,5,8,11,14,22-hexaoxo-17,18-dithia-1,4,7,10,13,21-hexazabicyclo[21.3.0]hexacosan-6-yl]acetic acid;N5-(aminoiminomethyl)-N2-(3-mercapto-1-oxopropyl)-L-arginylglycyl-L-alpha-aspartyl-L-alpha-trypotophyl-L-alpha-prolyl-L-alpha-cysteinamide,cyclic(1-6)-disulfide;
Batifiban is a synthetic peptidomimetic compound structurally designed to mimic the biological activity of natural integrin antagonists, making it a valuable research tool in the field of carbohydrate chemistry and platelet aggregation studies. Characterized by its unique molecular architecture, Batifiban exhibits high specificity for glycoprotein IIb/IIIa receptors, which are critical mediators of platelet adhesion and aggregation. Its stability and solubility profile render it suitable for a variety of in vitro experimental setups, ranging from cell-based assays to receptor-binding studies. As a non-peptide antagonist, Batifiban offers distinct advantages over traditional peptide-based inhibitors, including enhanced metabolic stability and a reduced likelihood of immunogenicity, thereby expanding its utility in research environments focused on thrombosis, hemostasis, and integrin-related cellular processes.
Platelet Aggregation Studies: Batifiban serves as a potent tool for investigating the molecular mechanisms underlying platelet aggregation. By selectively inhibiting the binding of fibrinogen to the glycoprotein IIb/IIIa complex on activated platelets, it enables researchers to dissect the specific pathways involved in thrombus formation. This application is particularly valuable for elucidating the contributions of integrin-mediated interactions in platelet function and for screening novel anti-aggregatory agents in preclinical research models.
Integrin Receptor Binding Assays: The compound's high affinity for glycoprotein IIb/IIIa receptors makes it an ideal candidate for use in integrin receptor binding assays. Batifiban allows for the quantitative measurement of receptor-ligand interactions, facilitating the study of structural requirements and binding kinetics of integrin antagonists. These assays are instrumental in drug discovery and development, as they provide insights into the efficacy and selectivity of new therapeutic candidates targeting integrin receptors.
Thrombosis Research Models: In the context of thrombosis research, Batifiban is frequently employed to model and analyze the inhibition of platelet-mediated clot formation in vitro. Its ability to block integrin-mediated platelet aggregation provides a controlled experimental platform for studying the pathophysiology of thrombotic disorders and evaluating the impact of potential antithrombotic agents. This application supports the development of safer and more effective therapeutic interventions for cardiovascular diseases associated with abnormal clot formation.
Cell Adhesion and Migration Studies: As a glycoprotein IIb/IIIa antagonist, Batifiban is also utilized in studies examining the role of integrins in cell adhesion and migration. By interfering with integrin-mediated cell-cell and cell-matrix interactions, it enables the investigation of cellular processes such as tissue remodeling, wound healing, and metastasis. This research direction is critical for understanding the broader implications of integrin signaling in both normal physiological and pathological conditions.
Signal Transduction Pathway Analysis: The use of Batifiban extends to the analysis of intracellular signaling pathways triggered by integrin activation. By inhibiting the initial binding events at the cell surface, researchers can delineate the downstream signaling cascades involved in platelet activation and aggregation. This application provides valuable mechanistic insights into the regulation of cellular responses to extracellular stimuli, contributing to the identification of novel molecular targets for therapeutic intervention.
Batifiban continues to be an indispensable asset in the toolkit of researchers exploring the intricate dynamics of integrin function, platelet biology, and carbohydrate-mediated cellular interactions. Its versatility across a spectrum of experimental paradigms underscores its importance in advancing scientific understanding of hemostatic and thrombotic processes, as well as in the broader study of integrin-related signaling and cellular behavior.
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