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 peptide compound recognized for its potent activity as a glycoprotein IIb/IIIa receptor antagonist, structurally designed to mimic the RGD (Arg-Gly-Asp) motif critical for platelet aggregation. As a cyclic peptide, it demonstrates high affinity and specificity for integrin receptors on platelets, making it a valuable tool in the study of thrombosis, hemostasis, and cell adhesion processes. Its well-defined biochemical properties and mechanism of action have positioned it as an important agent in both academic and industrial research focused on platelet function, vascular biology, and integrin-mediated cell signaling.
Platelet aggregation studies: Batifiban serves as a highly effective inhibitor in in vitro platelet aggregation assays, enabling researchers to dissect the molecular mechanisms underlying platelet activation and aggregation. By selectively blocking the interaction between fibrinogen and the glycoprotein IIb/IIIa receptor, it allows for precise evaluation of integrin-mediated platelet responses to various agonists. This application is critical for elucidating the pathways involved in hemostasis and for identifying potential modulators of platelet function in cardiovascular research.
Integrin receptor characterization: The compound's structural mimicry of the RGD sequence provides a robust tool for probing the specificity and binding dynamics of integrin receptors, particularly αIIbβ3. Researchers utilize Batifiban to map receptor-ligand interactions, quantify binding affinities, and investigate conformational changes in integrins upon ligand engagement. Such studies contribute to a deeper understanding of integrin biology and support the rational design of next-generation receptor antagonists.
Cell adhesion and migration assays: Batifiban's ability to disrupt integrin-mediated cell adhesion makes it a valuable reagent in studies examining the role of cell-matrix interactions in migration, spreading, and tissue remodeling. By inhibiting the binding of cells to extracellular matrix proteins, it helps clarify the contributions of specific integrins to cellular motility and invasion, with applications in vascular biology, oncology, and tissue engineering research.
Peptide drug development research: As a model cyclic peptide with defined receptor antagonism, Batifiban is frequently employed in the development and optimization of novel peptidomimetic compounds. Its structure-activity relationship data inform the design of synthetic analogs with improved stability, selectivity, or pharmacokinetic profiles. This supports medicinal chemistry efforts aimed at generating innovative integrin-targeted agents for research use.
Analytical method validation: The compound's well-characterized interaction with platelet integrins makes it a suitable positive control or reference standard in the validation of analytical assays, including flow cytometry, ELISA, and surface plasmon resonance techniques. Its consistent inhibitory activity provides a benchmark for assessing assay performance and for calibrating detection systems in laboratories focused on platelet biology and integrin research.
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