Eptifibatide, is an antiplatelet drug of the glycoprotein IIb/IIIa inhibitor class. Eptifibatide is a cyclic heptapeptide derived from a protein found in the venom of the southeastern pygmy rattlesnake (Sistrurus miliarius barbouri). It belongs to the class of the so-called RGD (arginine-glycine-aspartate)-mimetics and reversibly binds to platelets.
CAT No: 10-101-15
CAS No:188627-80-7 (net)
Synonyms/Alias:Eptifibatide; Integrilin; CHEBI:291902
Chemical Name:2-[20-carbamoyl-12-[4-(diaminomethylideneamino)butyl]-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
Eptifibatide Acetate is a cyclic heptapeptide belonging to the class of synthetic peptide inhibitors targeting platelet aggregation pathways. Structurally derived from a component of rattlesnake venom, it is characterized by its specific affinity for the glycoprotein IIb/IIIa receptor on platelets, making it a potent and selective modulator of integrin-mediated cellular interactions. Its molecular design and biological activity have rendered it an indispensable tool in platelet biology research, integrin signaling studies, and the broader exploration of thrombosis and hemostasis mechanisms. The compound's high specificity and reversible binding profile provide researchers with a valuable model for dissecting the molecular underpinnings of platelet function and for developing advanced antithrombotic strategies.
Platelet Aggregation Research: Eptifibatide Acetate is extensively utilized in studies investigating the mechanisms of platelet aggregation and activation. By selectively antagonizing the glycoprotein IIb/IIIa receptor, it enables precise modulation of fibrinogen binding and subsequent platelet cross-linking. Researchers employ this peptide to elucidate the sequence of events leading to thrombus formation, to validate the role of integrin-mediated signaling in hemostasis, and to distinguish between primary and secondary platelet activation pathways under a variety of experimental conditions.
Integrin Function Analysis: The compound serves as a robust tool for probing the structure-function relationships of integrin receptors, particularly αIIbβ3. Its well-characterized mode of action allows for the dissection of ligand-receptor interactions at the molecular level. Scientists leverage eptifibatide's competitive binding properties to map critical residues involved in ligand recognition, to study conformational changes upon ligand engagement, and to assess the downstream signaling cascades initiated by integrin activation or inhibition in both platelets and other integrin-expressing cells.
Thrombosis Model Development: Eptifibatide Acetate is frequently incorporated into in vitro and ex vivo models of thrombosis to simulate and manipulate the dynamics of clot formation. Its reversible inhibition of platelet aggregation is particularly valuable in the development and validation of experimental systems designed to evaluate the efficacy of novel antithrombotic agents, to study the interplay between coagulation factors and cellular elements, and to investigate the impact of genetic or pharmacological interventions on thrombotic risk.
Flow Cytometry and Platelet Function Testing: The peptide's high specificity for the glycoprotein IIb/IIIa receptor makes it a preferred reagent in advanced platelet function assays, including flow cytometry-based analyses. By selectively blocking integrin-mediated aggregation, eptifibatide enables the quantification of residual platelet reactivity, facilitates the discrimination of surface marker expression, and supports the assessment of platelet responses to various agonists or inhibitors. These applications are critical for both basic research and the optimization of diagnostic protocols in laboratory settings.
Drug Discovery and Screening: Eptifibatide Acetate is an essential reference compound in the development and screening of new platelet aggregation inhibitors and antithrombotic agents. Its well-documented pharmacological profile provides a benchmark for evaluating the potency, selectivity, and reversibility of candidate molecules targeting the glycoprotein IIb/IIIa pathway. The compound is routinely employed in high-throughput screening assays, structure-activity relationship studies, and the optimization of lead compounds within the context of integrin-targeted drug discovery programs.
Protein disulfide isomerase (PDI) catalyzes the oxidation reduction and isomerization of disulfide bonds. We have previously identified an important role for extracellular PDI during thrombus formation in vivo. Here, we show that endothelial cells are a critical cellular source of secreted PDI, important for fibrin generation and platelet accumulation in vivo. Functional PDI is rapidly secreted from human umbilical vein endothelial cells in culture upon activation with thrombin or after laser-induced stimulation. PDI is localized in different cellular compartments in activated and quiescent endothelial cells, and is redistributed to the plasma membrane after cell activation. In vivo studies using intravital microscopy show that PDI appears rapidly after laser-induced vessel wall injury, before the appearance of the platelet thrombus. If platelet thrombus formation is inhibited by the infusion of eptifibatide into the circulation, PDI is detected after vessel wall injury, and fibrin deposition is normal. Treatment of mice with a function blocking anti-PDI antibody completely inhibits fibrin generation in eptifibatide-treated mice. These results indicate that, although both platelets and endothelial cells secrete PDI after laser-induced injury, PDI from endothelial cells is required for fibrin generation in vivo.
Jasuja, R., Furie, B., & Furie, B. C. (2010). Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo. Blood, 116(22), 4665-4674.
The objective of the study was to determine the identity of a new impurity detected in HPLC chromatograms of research samples of eptifibatide manufactured by a new process and formulated into drug product. The identification of the unknown impurity was required in order to understand the mechanism of its formation. The analysis was performed by using tandem mass spectrometers coupled with a reversed-phase gradient HPLC system. The unknown compound was then structurally elucidated by matrix-assisted laser desorption ionization (MALDI) tandem mass spectrometry. The mass spectrometric results showed that the protonated molecular ion of the unknown compound was m/z 862.3347 with molecular formula: C(36)H(52)N(11)O(10)S(2). The unknown compound was a linear peptide and was related to Asp-clipped eptifibatide. It was formed from Asp-clipped eptifibatide by the reaction of the amino group of tryptophan moiety with formaldehyde followed by electrophilic attack on the nitrogen of indole.
Wang, R., Feder, D., & Hsieh, F. (2003). Characterization of eptifibatide during drug formulation stability assays. Journal of pharmaceutical and biomedical analysis, 33(5), 1181-1187.
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