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  • ISSN: 2379-089X
    Volume 2, Issue 2
    Research Article
    Shailendra Bhatt1*, Divya Sharma1, Shailendra Mandge2, Swapnil Sharma3 and Vikas Jain4
    Abstract: The purpose of this work was to develop taste masked fast dissolving tablets of Ondansetron HCl that overcomes principle drawback of such formulations, which is slow disintegration and inadequate mechanical strength. In the present work taste masked Ondansetron HCl fast dissolving tablets were formulated and optimized by using different ratio of MCC in MCC: Lactose combination and different concentration of Ac-Di-Sol. A 32 full factorial design and statistical models were applied to optimize the effect of two factors. It was observed that the responses, i.e., disintegration time and hardness were affected by both the factors. The statistical models were validated and can be successfully used to prepare fast dissolving tablets of Ondansetron HCl with rapid disintegration (24 seconds) and excellent mechanical strength (4.4 kg/cm2). Pharmacokinetic studies in rats showed statistically insignificant difference (p>0.05) between OFDT1 and marketed product (Ondem MD 8), concluded that optimized FDT was found to be bioequivalent in rate and extent of absorption with the marketed formulation. While, The values of Tmax were found to be 1 h and 2 h for OFDT1 and Ondem MD8, respectively, showed quick onset of action with OFDT1. Stability studies was performed on optimize tablet and it was concluded that formulations were stable and no significant change in the percentage drug content, hardness, disintegration time and drug release was to be observed.
    Perspective
    Alastair D.G. Lawson* and Benjamin P
    For Structure-based Drug Discovery to guide Medicinal Chemistry in real time, the underlying crystal structures must be reliable and representative of the relevant molecular conformation of the protein being targeted by the small molecule.While X-ray crystallography continues to be the gold standard for high resolution structural studies, crystallisable forms of the protein may not always coincide with the desired biologically relevant conformation [1].
    Short Communication
    Anna Pielesz
    In the current researches microbiological procedure, cellulose acetate electrophoresis, Fourier-transform infrared spectrometry and Scanning electron microscopy were all carried out after heating samples of chicken skin to a temperature simulating a burn incident and stimulate the release of Heat Shock Proteins. The objective of this study was to monitor the effect of temperature on collagen from organic chicken skins, which was used as a model of ex-vivo burn injured skin. Aggregates of smaller molecular weight, probably Heat Shock Proteins 37 (HSP37) proteins which undergo atrophy in presence of hydro gels like H4SiO4 × nH2O or L-Ascorbic Acid solution, were isolated by cellulose acetate electrophoresis. The examples of FTIR spectra were recorded from frozen samples of thermally modified serum.
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