Study on the thermal stability of nab-paclitaxel during hyperthermic intraperitoneal chemotherapy
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Abstract Background Albumin-bound paclitaxel (nab-paclitaxel), as a special targeted preparation of paclitaxel, has the advantages of good curative effect and less side effects in anti-tumor therapy. The existence of the plasma-peritoneal barrier and insufficient blood supply make intravenous drugs hard to reach the peritoneum, while hyperthermic intraperitoneal chemotherapy can solve the difficulty. And compared with systemic medications, HIPEC can also give higher concentrations of chemotherapy drugs in the abdominal cavity, while ensuring lower systemic toxicity. However, at present, there is no relevant report on the clinical study of nab-paclitaxel during intraperitoneal hyperthermic chemotherapy, and its stability under special temperature conditions has not been reported either. Methods In this study, We examined three batches of albumin-bound paclitaxel dissolved in saline at different temperatures (25 °C, 37 °C, 41 °C, 42 °C and 43 °C) for the changes of human serum albumin content, human serum albumin polymer content, related substance content, in-vitro release rate, paclitaxel binding rate and paclitaxel content at different temperatures. Results Our results demonstrated that the indicators including human serum albumin content, human serum albumin polymer content, in-vitro release rate, paclitaxel binding rate and paclitaxel content were stable to the several temperatures, except that Taxane (0.1%) and other individual impurities in the determination of related substance content fluctuated comparatively widely with the change of temperature. In addition, only Taxane (0.1%) and 7-Epitaxol (1%) were detected. Conclusions Overall, albumin-bound paclitaxel is relatively stable to different temperatures (25 °C, 37 °C, 41 °C, 42 °C and 43 °C). This study will lay a foundation for further studies on the albumin-bound paclitaxel during hyperthermic intraperitoneal chemotherapy.Keywords:
Taxane
Human serum albumin
Hyperthermic Intraperitoneal Chemotherapy
Serum Albumin
Sera from patients undergoing hemodialysis with formaldehyde (F)-sterilized dialyzers were studied to determine if antibodies against F conjugated to human serum albumin (HSA) could be detected. F-human serum albumin (F-HSA) conjugates were prepared using ratios of F to HSA that did not precipitate the HSA. The F-HSA conjugates migrate differently electrophoretically than HSA with an increased negative charge of F-HSA as compared with HSA. The F-HSA was used in an ELISA. The results demonstrated that in certain sera, IgG, IgM, IgA and IgE antibodies against F-HSA could be measured. In the highest titered sera, it was shown that the IgG antibody was not directed against F alone or F-lysine but against an antigenic grouping of F-HSA. No correlation of either IgG or IgE antibodies with immune complex or allergic reactions was found in this series of dialysis patients. Some sera from dialysis patients had antibody activity against HSA. Sera from 2 physicians with rhinitis after F exposure had no antibody activity against F-HSA or HSA. Two nurses with a history of F-induced asthma had no IgG antibodies but did have IgE antibodies against F-HSA and HSA. This spectrum of immunologic responses is analogous to responses in dogs immunized with F or F dog albumin. We have not been able to identify anti HSA antibodies in patients reactive to other hapten-HSA compounds and it is suggested that anti HSA antibodies in F-exposed humans may relate to the F exposure.
Human serum albumin
Serum Albumin
Hapten
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Correlation between binding parameters of 6 benzodiazepines to free human serum albumin (HSA) and chromatographic retention parameters on the HSA stationary phase (HSA-SP) was better than the similar correlation with alpha-1-acid glycoprotein (AGP). Still better correlation was obtained between binding to both proteins and retention on an octadecylsilane (ODS) column. For 12 benzodiazepines the correlations of the retention parameters on both protein columns with the retention on the ODS column were additionally investigated. In the case of HSA this correlation was good.
Human serum albumin
Orosomucoid
Serum Albumin
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The binding of thioridazine and some of its psychoactive metabolites to human serum and to human albumin was studied using equilibrium dialysis. A very important binding capacity was found for each of the products tested, but significant differences between binding to human serum and binding to human albumin were observed.
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The binding of glycyrrhizin (GLZ) to human serum and human serum albumin (HSA) was examined by an ultrafiltration technique. Specific and nonspecific bindings were observed in both human serum and HSA. The association constants (K) for the specific binddings were very similar : 1.31×105M-1 in human serum and 3.87×105M-1 in HSA. The number of binding sites (n) and the linear binding coefficient (Φ) in HSA were 1.95 and 3.09×103M-1, respectively.When the human serum protein concentration ws assumed to be 4.2% (equal to the measured serum albumin concentration), n in human serum was 3.09, which is similar to the n value in HSA, and Φ in human serum was 0.71×103M-1, which is reasonably close to that for HSA. The binding pattern of GLZ with human serum protein on Sephadex G-200 column chromatography showed that GLZ binds to only the albumin fraction.It was concluded that the GLZ-binding sites in human serum exist mainly on albumin and GLZ binds to specific and nonspecific binding sites at lower and higher concentrations that approximately 2mM, respectively.
Human serum albumin
Glycyrrhizin
Sephadex
Serum Albumin
Ultrafiltration (renal)
Human albumin
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In order to identify the effect of temperature on the content of Taxol and Taxane extracted from fresh leaf and green branch of Taxus yunnanensis,the test was made for Taxol and Taxane pretreated under different temperatures by using high performance liquid chromatograph. The result showed that there was no significant impact from drying temperature on the content of Taxol and Taxane. However,the appropriate drying temperature could be90℃ with 60 min in practice.
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Objective: This exploratory study aimed to evaluate and compare the treatment costs of taxane-based versus cisplatin-based chemotherapy.Methods: This study used data from the medical and financial records of ovarian cancer patients who were admitted to Dharmais NationalCancer Hospital (RSKD) between 2008 and 2012 and subsequently underwent surgery and were treated with chemotherapy. Data were analyzedusing descriptive analysis, and a Kaplan–Meier graph was plotted to compare the survival of the patients in the taxane-based and cisplatin-basedchemotherapy groups.Results: Of 41 patients, treatment costs were available for nine patients who had undergone taxane-based chemotherapy and for 31 patients who hadundergone cisplatin-based chemotherapy. In general, surgical procedures accounted for the highest proportion of the treatment costs, followed bychemotherapy. Taxane-based chemotherapy (six cycles) was 4 times more expensive than cisplatin-based therapy. The pre- and post-chemotherapycosts of care among those treated with the taxane-based regimen were 3-4 times more expensive than those of the patients who received cisplatinbasedtreatment. The disease-free recurrence duration of the patients treated with taxane was longer (median=18 months) than that of the patientstreated with cisplatin (median=5 months).Conclusions: Taxane-based therapy increased the disease-free recurrence duration of the patients, with disease-free recurrence 3 times longer thanthat of the patients treated with the cisplatin-based regimen. However, the treatment costs of the taxane-based regimen were 4 times higher thanthose of the cisplatin-based treatment.
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Taxus L species (yews) are the primary source of the leading anticancer agent taxol and generally of antineoplastic taxanes. As taxane demands exceed supply new sources, such as the marginal south-eastern T. baccata populations in Greece, are explored. Results of a metabolic (UPLC-MS/MS, MRM) analysis of taxane content of two populations (Mt Cholomon, Mt. Olympus) showed no significant differences in paclitaxel production, but the docetaxel and paclitaxel precursor DAB was significantly higher Mt Cholomon by 29.83%. Higher yielding paclitaxel trees (HYT) appear to be lower yielding in DAB at the population level: the 10 paclitaxel HYT of Mt. Cholomon produced 25% less that the 10 HYT of Mt. Olympus, while the 10 DAB HYT trees of the former produced 14% more than the 10 HYT of the latter. Populations presented taxane concentrations on the low end of the range reported in the literature (paclitaxel 1.1–5.7 mg 100-1g dw; DAB 12.7-81.1 mg 100-1g dw). Notable levels of genetic (SSR) and epigenetic (MSAP) diversity were found in both populations; the former were lower though than values reported in other relevant studies for Taxus (SSR). Preliminary analyses on the relations of genetic and epigenetic diversity to HYT and LYT for both taxanes were inconclusive. This analysis presents a first insight regarding the potential of future commercial exploitation of these genetic resources for taxol production.
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Human serum albumin
Serum Albumin
Human albumin
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Human serum albumin
Serum Albumin
Bovine serum albumin
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The binding of glycyrrhetinic acid (GLA) to rat plasma, rat serum albumin (RSA), human serum, and human serum albumin (HSA) was examined by an ultrafiltration technique. Specific and nonspecific bindings were observed in all cases. The assosiation constant (K) for the specific binding was 1.34 × 105 M-1 in rat plasma and 1.56 × 105 M-1 in RSA. The K value for human serum (14.91 × 105 M-1) and that for HSA (15.09 × 105 M-1) were approximately 10-fold larger than those for rat plasma and RSA, suggesting a species difference in the specific binding affinity for GLA. The number of specific binding sites (n) was 2.49 and 1.18 for RSA and HSA, respectively. The linear binding coefficient (ψ) for the nonspecific binding was 7.11 × 103 M-1 in RSA and 6.57 × 103 M-1 in HSA.When the rat plasma and human serum protein concentrations are respectively assumed to be 3.5% and 4.2% (equal to the measured plasma and serum albumin concentrations), n was 1.83 in rat plasma and 1.31 in human serum, which corresponded fairly well to those for RSA and HSA. Further, for ψ in rat plasma and human serum, when rat plasma and human serum protein are the measured albumin concentrations, respectively, ψ was 10.97 × 103 M-1 for rat plasma and 14.83 × 103 M-1 for human serum, which corresponded well to those for RSA and HSA.It was concluded that the GLA-binding sites in rat plasma and human serum exist in albumin and GLA binds to specific and nonspecific binding sites at lower and higher concentrations than approximately 2 mM, respectively.
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Serum Albumin
Ultrafiltration (renal)
Blood plasma
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