“…The development of enzyme-linked immunoassays [111,112] and a fluoroimmunoassay [113] for quantification of paclitaxel in biological samples has been described (SupplemenTary Table 7). These immunoassays utilize the binding of paclitaxel to antibodies for quantification of paclitaxel.…”
Since the isolation of paclitaxel and its approval for the treatment of breast cancer, various taxanes and taxane formulations have been developed. To date, almost 100 bioanalytical assays have been published with the method development and optimization often extensively discussed by the authors. This Review presents an overview of assays published between January 1970 and September 2013 that described method development and validation of assays used to quantify taxanes in biological matrices such as plasma, urine, feces and tissue samples. For liquid chromatography assays, sample pretreatment, chromatographic separation and assay performance are compared. Since this Review discusses the limitations of previously developed liquid chromatography assays and gives recommendations for future assay development, it can be used as a reference for future development of liquid chromatography assays for the quantification of taxanes in various biological matrices to support preclinical and clinical studies.
“…The development of enzyme-linked immunoassays [111,112] and a fluoroimmunoassay [113] for quantification of paclitaxel in biological samples has been described (SupplemenTary Table 7). These immunoassays utilize the binding of paclitaxel to antibodies for quantification of paclitaxel.…”
Since the isolation of paclitaxel and its approval for the treatment of breast cancer, various taxanes and taxane formulations have been developed. To date, almost 100 bioanalytical assays have been published with the method development and optimization often extensively discussed by the authors. This Review presents an overview of assays published between January 1970 and September 2013 that described method development and validation of assays used to quantify taxanes in biological matrices such as plasma, urine, feces and tissue samples. For liquid chromatography assays, sample pretreatment, chromatographic separation and assay performance are compared. Since this Review discusses the limitations of previously developed liquid chromatography assays and gives recommendations for future assay development, it can be used as a reference for future development of liquid chromatography assays for the quantification of taxanes in various biological matrices to support preclinical and clinical studies.
“…Tubulin‐based biochemical assay is characterized by a minimal pre‐treatment of sample but its sensitivity is limited compared to LC‐UV and LC‐MS methods (Hamel et al, ; Morais et al, ). Even if immunoassays (Grothaus et al, ; Svojanovsky et al, ; Sheikh et al, ) are characterized by a good LOQ (below 0.5 ng/mL), this method could be invalidated by cross reactivity of metabolites to antibodies resulting in decreasing of concentration accuracy. MEKC combines chromatographic and electrophoretic separation principles and the separation is based on the differential partitioning of an analyte between the two‐phase system: the mobile aqueous phase and micellar pseudostationary phase.…”
Section: Classes Of Anticancer Natural Productsmentioning
“…Reports have demonstrated that a capillary immunosensor can be utilized for the analysis of heart marker proteins: myoglobin, creatine kinase mb, troponin I, and fatty acid-binding protein, 18,19 and for the measurement of paclitaxel, an anticancer drug. 20,21 However, most capillary immunosensors are used primarily in automated systems, they therefore require a flow-through process with reagents on the sub-milliliter order. Thus, even in the capillary immunosensors, they consume large amounts of expensive reagents and precious samples.…”
To simplify the complicated operation steps and to minimize sample and reagent amounts for enzyme-linked immunosorbent assays (ELISA), we developed a square glass capillary immunosensor containing both covalently immobilized capture antibodies and physically adsorbed enzyme-linked antibodies. The immobilization of capture antibodies (anti-human IgG) was carried out by the treatment of 3-aminopropyltriethoxy silane, glutaraldehyde, and protein-A, followed by affinity capture of the antibody. In contrast, the enzyme-linked antibodies (alkaline phosphatase (ALP)-linked anti-human IgG) were physically adsorbed on the four corners of the capillary with the aid of polyethylene glycol (PEG) acting as a scaffold. A nanoliter volume of antigen (human IgG)-containing sample solution was introduced via capillary action. This addition resulted in the release and diffusion of ALP-linked anti-human IgG into the bulk solution. This event led to a 20-min single-step sandwich immunoreaction at the inner wall of capillary; the reaction was detected through the reaction with fluorescein diphosphate (FDP) which generated a fluorescent product, fluorescein. Using this technique, we obtained an intra-capillary precision with a coefficient of variation of 9.7%. In addition, the specificity study showed that the human IgG capillary immunosensor did not respond to rabbit IgG. Quantitative analysis was possible within the response range of 10 - 5000 ng mL(-1) anti-human IgG. This capillary immunosensor can act as a single analytical unit or can be integrated into a capillary array for multiple bioanalysis.
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