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, a synthetic cyclic heptapeptide derived from a component found in rattlesnake venom, is recognized for its potent inhibitory effect on platelet aggregation. As a selective antagonist of the glycoprotein IIb/IIIa receptor on platelets, Eptifibatide Acetate is widely studied in the context of cardiovascular research and thrombosis models. Its unique structure allows for reversible binding, making it a valuable tool in both in vitro and in vivo investigations that require precise modulation of platelet activity. The compound's high specificity and well-characterized mechanism of action have positioned it as a cornerstone molecule in the exploration of platelet-mediated processes, providing researchers with a reliable means to dissect the intricacies of platelet function and thrombus formation. Its solubility and stability under experimental conditions further enhance its utility across a broad spectrum of laboratory settings, ensuring reproducibility and consistency in scientific outcomes.
Antithrombotic Research: Eptifibatide Acetate is extensively employed in antithrombotic research to elucidate the pathways involved in platelet aggregation and thrombus development. By selectively inhibiting the glycoprotein IIb/IIIa receptor, it allows researchers to model and evaluate the efficacy of novel antiplatelet agents or therapeutic strategies in preclinical settings. Its reversible action is particularly advantageous for studying the temporal dynamics of platelet inhibition and recovery, enabling detailed assessment of drug interactions and potential synergistic effects in combination therapies. The compound's ability to mimic physiological conditions makes it indispensable for advancing the understanding of thrombosis mechanisms and for screening new molecules that target platelet aggregation.
Platelet Function Assays: In the realm of platelet function assays, Eptifibatide serves as a reference inhibitor for validating assay performance and for standardizing experimental protocols. Its well-documented inhibitory profile enables precise calibration of platelet aggregation responses, which is critical for the development and optimization of diagnostic tools. Researchers utilize it to establish baseline levels of platelet inhibition, compare the potency of emerging antiplatelet compounds, and troubleshoot variability in assay results. The compound's consistency across different assay formats—such as light transmission aggregometry and flow cytometry—ensures reliable benchmarking and contributes to the reproducibility of platelet function studies.
Cardiovascular Disease Models: Eptifibatide Acetate is frequently incorporated into experimental models of cardiovascular disease, where it serves as a tool to dissect the role of platelet aggregation in pathological conditions such as myocardial infarction and stroke. Its targeted mechanism of action allows scientists to simulate the effects of platelet inhibition in animal models, providing valuable insights into the interplay between hemostasis, thrombosis, and vascular injury. By modulating platelet activity, researchers can investigate the downstream effects on tissue perfusion, inflammation, and recovery, thereby enhancing the translational relevance of their findings to human cardiovascular health.
Biomaterials and Medical Device Testing: The application of Eptifibatide extends to the evaluation of biomaterials and the hemocompatibility of medical devices. In this context, it is used to assess the propensity of surfaces to induce platelet adhesion and aggregation, which are critical factors in the design of vascular grafts, stents, and extracorporeal circuits. By inhibiting platelet activation, the compound helps researchers distinguish between material-induced and physiological platelet responses, facilitating the development of safer and more effective medical devices. Its use in standardized testing protocols supports the identification of surface modifications that minimize thrombogenicity without compromising device function.
Signal Transduction Studies: Eptifibatide Acetate is also instrumental in signal transduction studies focused on platelet activation pathways. By blocking the final common pathway of platelet aggregation, it enables researchers to isolate upstream signaling events and dissect the contributions of various agonists and receptors. This approach is particularly valuable for mapping intracellular signaling cascades, identifying novel therapeutic targets, and understanding the molecular basis of platelet-related disorders. The compound's specificity and reversible action make it an ideal tool for dynamic studies that require temporal control over platelet inhibition, supporting the advancement of knowledge in cellular signaling and platelet biology.
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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