ABSTRACT
Miconazole is a widely used antifungal agent with poor aqueous solubility, which requires the development of drug delivery systems able to improve its therapeutic activity. For this purpose, a miconazole-loaded nanostructured lipid carriers (NLC) dispersion was prepared and characterized. Further, the dispersion was used to prepare a NLC-based hydrogel formulation proposed as an alternative system to improve the local delivery of miconazole to the oral mucosa. NLC dispersion showed particles in the nanometer range (≈ 200 nm) with low polidispersity index (<0.3), good physical stability and high encapsulation efficiency (>87%). A controlled miconazole release was observed from NLC and NLC-based hydrogel formulations, in contrast to a commercial oral gel formulation, which demonstrated a faster release. Additionally, it was observed that the encapsulation of miconazole in the NLC improved its antifungal activity against Candida albicans. Therefore, it was demonstrated that the encapsulation of miconazole in NLC allows for obtaining the same therapeutic effect of a commercial oral gel formulation, using a 17-fold lower dose of miconazole.
Subject(s)
Antifungal Agents/pharmacology , Drug Carriers/chemistry , Drug Delivery Systems , Lipids/chemistry , Miconazole/pharmacology , Mouth Mucosa/drug effects , Nanostructures/chemistry , Calorimetry, Differential Scanning , Candida albicans/drug effects , Chemistry, Pharmaceutical , Crystallization , Hydrogels/pharmacology , Kinetics , Particle Size , Placebos , Rheology/drug effects , Static ElectricityABSTRACT
A monosegmented flow system is designed for enzymatic spectrophotometric determination of cholesterol in blood serum. The sample (4.5 microliters), enzymatic reagent (150 microliters) and an air plug (100 microliters) are simultaneously inserted into a carrier stream buffered to pH 7.4 (potassium dihydrogenphosphate). In order to avoid the step of air removal, a relocating detector was used. This system handles about 42 samples per hour, yielding precise results (R.S.D. usually < 3.0%). Sensitivity is 46 mAU 1/mmol (mAU stands for milliabsorbance units), being the method linear up to 10.3 mmol/l cholesterol. Accuracy was assessed by running 30 samples already analysed by a conventional procedure: no statistical difference between methods was found at the 95% confidence level.
Subject(s)
Cholesterol/blood , Buffers , Flow Injection Analysis , Humans , Hydrolysis , Indicators and Reagents , SolutionsABSTRACT
Systemic lupus erythematosus autoantibodies were used to identify and to characterize new human chromosome-associated proteins. Previous immunolocalization studies in human and murine tissue culture cells showed that some of these monoclonal antibodies recognize nuclear antigens that associate with condensed chromosomes during mitosis. One antibody was selected for screening a human HeLa S3 cDNA expression library, and cDNAs that code for an antigen of 31-33 kDa were isolated. Immunological, biochemical and cell fractionation data indicate that the 31- to 33-kDa antigen corresponds to the chromosome-associated protein recognized by the original monoclonal antibody. Sequence analysis shows that we isolated a novel human gene. Immunolocalization to human tissue culture cells shows that during interphase the antigen is dispersed in the nucleus and that during mitosis it associates exclusively with condensed chromosomes. A similar pattern of localization was also observed in mouse fibroblasts, suggesting that the antigen is conserved among different species. Finally, we show that part of the antigen remains bound to the scaffold/matrix component, even after high salt extraction.
