A double antibody radioimmunoassay for the determination of XV459, the active hydrolysis metabolite of roxifiban, in human plasma

Pieniaszek, Henry J.; Davidson, Anna F.; Walton, Harry L.; Pinto, Donald; Olson, R. E.; Reilly, Thomas M.; Barrett, Yu Chen

doi:10.1016/s0731-7085(02)00481-8

Cited by 7 publications

(4 citation statements)

References 3 publications

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“…Merck (West Point, PA, USA) provided tirofiban hydrochloride (Aggrastat ® ; l ‐tyrosine‐ N ‐[butylsulfonyl]‐ O ‐[‐4–4(piperidinebutyl)] monohydrochloride); concentrations were determined spectrally [32,33]. DuPont Pharmaceuticals (Wilmington, DE, USA) provided the roxifiban metabolites XV549 (methyl N 3 ‐[2‐{3‐(4‐formamidino‐phenyl)‐isoxazolin‐5(R)‐yl}‐acetyl]‐ N 2 ‐(1‐butyloxycarbonyl)‐2,3‐(S)‐diaminopropionate) [34], XP280, the benzene sulfonate salt of XV459 [35], and orbofiban (ethyl 3‐[[[[1‐[4(aminoiminomethyl)phenyl]‐2‐oxo‐3S pyrrolidinyl]amino]carbonyl]amino]‐propanoate, acetate salt) [36]; concentrations were determined by dry weight. Highly purified human fibrinogen was purchased from American Diagnostica (Greenwich, CT, USA) and highly purified human α ‐thrombin from Sigma Chemicals (St Louis, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

αIIbβ3 priming and clustering by orally active and intravenous integrin antagonists

Hantgan

Stahle

Connor

et al. 2007

Journal of Thrombosis and Haemostasis

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Summary. Background: Drugs that block platelet-platelet and platelet-fibrin interactions via the a IIb b 3 (glycoprotein IIb/IIIa) receptor are used daily in patients undergoing percutaneous coronary interventions. Along with expected increases in spontaneous bleeding, clinical trials have revealed a surprising increase in thrombosis when these drugs are used without other anticoagulants. A better understanding of their mechanisms can minimize these risks. Objectives: This study tested the hypothesis that interventions designed to block fibrinogen binding inevitably leave the a IIb b 3 receptor in an activated state. It compared the effects on platelet function and a IIb b 3 conformation of the orally active compounds orbofiban and roxifiban, the i.v. agents eptifibatide and tirofiban, and echistatin, an arginine-glycine-aspartate (RGD) disintegrin. Methods: The integrin antagonist concentrations required to saturate platelets and to block plateletplatelet and platelet-fibrin interactions were determined by flow cytometery, aggregometry, and clot-based adhesion assays, respectively. Analytical ultracentrifugation measured each antagonist's effects on the solution structure of a IIb b 3 . Fluorescence anisotropy provided equilibrium and kinetic data for integrin:antagonist interactions. Results: Both orally active drugs bound more tightly and inhibited platelet aggregation and adhesion to fibrin more effectively than echistatin. Analytical ultracentrifugation yielded this order for perturbing a IIb b 3 conformation (priming) and promoting oligomerization (clustering):echistatin > eptifibatide > orbofiban > tirofiban > roxifiban. Roxifiban was also most effective at disrupting the rapidly forming/slowly dissociating a IIb b 3 :echistatin complex. Conclusions: Our results suggest that the same molecular mechanisms that enable glycoprotein IIb/IIIa inhibitors to bind tightly to the a IIb b 3 receptor and block fibrinogen binding contribute to their ability to perturb the resting integrin's conformation, thus limiting the safety and efficacy of both oral and i.v. integrin antagonists.

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Section: Methodsmentioning

confidence: 99%

αIIbβ3 priming and clustering by orally active and intravenous integrin antagonists

Hantgan

Stahle

Connor

et al. 2007

Journal of Thrombosis and Haemostasis

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“…Immunoassay methods are important pharmaceutical analytical tools for diagnosing diseases, detecting toxins, therapeutic drug monitoring, as well as clinical pharmacokinetics and bioequivalence studies in drug discovery and pharmaceutical development ( Findlay et al, 2000 ). Immunoassays results have extremely high sensitivities and low limits of detection ( Pieniaszek et al, 2003 ; Suzuki et al, 2003 ). Although antibodies and other signal generating labels are used for immunoassay development, antibodies are undoubtedly the key reagents ( Darwish, 2006 ).…”

Section: Introductionmentioning

confidence: 99%

Current Demands for Food-Approved Liposome Nanoparticles in Food and Safety Sector

et al. 2017

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Safety of food is a noteworthy issue for consumers and the food industry. A number of complex challenges associated with food engineering and food industries, including quality food production and safety of the food through effective and feasible means can be explained by nanotechnology. However, nanoparticles have unique physicochemical properties compared to normal macroparticles of the same composition and thus could interact with living system in surprising ways to induce toxicity. Further, few toxicological/safety assessments have been performed on nanoparticles, thereby necessitating further research on oral exposure risk prior to their application to food. Liposome nanoparticles are viewed as attractive novel materials by the food and medical industries. For example, nanoencapsulation of bioactive food compounds is an emerging application of nanotechnology. In several food industrial practices, liposome nanoparticles have been utilized to improve flavoring and nutritional properties of food, and they have been examined for their capacity to encapsulate natural metabolites that may help to protect the food from spoilage and degradation. This review focuses on ongoing advancements in the application of liposomes for food and pharma sector.

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“…[14][15][16][17] Enzyme-linked immunosorbent assay (ELISA), the most versatile format of immunoassays, is remarkably quick and is easily performed, yielding information that would be difficult to obtain by the chromatographic methods, and also offers great sensitivity when an appropriate enzyme label is used. [16][17][18][19] In addition, ELISA, as it uses analyte-specific antibodies, does not require pretreatment for the samples, and it is well suited for screening of large number of samples. [20][21][22] The specificity of the antibody to the analyte of interest is the limiting factor in the validity of any ELISA system.…”

Section: Introductionmentioning

confidence: 99%

Generation of a Specific Polyclonal Antibody With High Affinity to Atorvastatin and Its Employment in the Development of Elisa for Determination of Atorvastatin in Plasma

Darwish

Al‐Obaid

Al-Malaq

2011

Journal of Immunoassay and Immunochemistry

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For the first time, a polyclonal antibody with high affinity to atorvastatin (ATR) was generated. The high specificity of the antibody for ATR among its structural analogues and co-administered therapeutic agents was proved. The antibody was employed in the development of enzyme-linked immunosorbent assay for quantitation of ATR in plasma. The assay was validated over a working range of 0.2-5 ng/mL. The intra- and interassay precisions were satisfactory; the coefficients of variations were ≤5%. The accuracy of the method was proved as the mean recovery was 96.4 ± 4.3%. The assay can be used in therapeutic monitoring and pharmacokinetic studies for ATR.

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A double antibody radioimmunoassay for the determination of XV459, the active hydrolysis metabolite of roxifiban, in human plasma

Cited by 7 publications

References 3 publications

αIIbβ3 priming and clustering by orally active and intravenous integrin antagonists

αIIbβ3 priming and clustering by orally active and intravenous integrin antagonists

Current Demands for Food-Approved Liposome Nanoparticles in Food and Safety Sector

Generation of a Specific Polyclonal Antibody With High Affinity to Atorvastatin and Its Employment in the Development of Elisa for Determination of Atorvastatin in Plasma

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