In order to develop a niosome-encapsulated ciprofloxacin (CPFX) HCl formulation for pulmonary delivery, the feasibility of encapsulation of CPFX in niosomes, its stability and nebulization capability was evaluated. Various combinations of nonionic surfactants with cholesterol were used to prepare the formulations. The in vitro deposition data of the niosomal formulations were examined using an Andersen cascade impactor. Formulations composed of Span 60 and Tween 60 in combination with 40 mol% of cholesterol exhibited high encapsulation efficacy and stability and also had fine particle fraction and nebulization efficiency of about 61.9% ± 1.0 and 77.9 ± 2.8, respectively. Minimal inhibitory concentration of the niosomal CPFX against some pulmonary pathogens were lower than free CPFX. Using the MTT assay in human lung carcinoma cell line (A549), niosome-entrapped CPFX showed significantly lower cytotoxicity in comparison to the free drug. These results indicate that niosome can be used as a carrier for pulmonary delivery of CPFX via nebulization.

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Objectives Immunotherapy using recombinant monoclonal antibodies specifically Anti-amyloid-beta (Anti-Aβ) scFv is envisaged as an appropriate therapeutic for Alzheimer through reduction of amyloid-beta aggregation. The solubilization of therapeutics using polymeric micelles facilitates an improved bioavailability and extended blood half-life. In this study, the optimum production condition for Anti-amyloid-beta (Anti-Aβ) scFv was obtained. To increase the stability of plasma, Anti-Aβ-loaded polymeric micelles were synthesized. Methods Escherichia coli SHuffle expression strain was used and purified by Ni-NTA. Pluronics P85 and F127 micelles were used for the Anti-Aβ delivery and were characterized in terms of morphology, drug loading and drug release in phosphate buffer and artificial cerebrospinal fluid. The stability profile was quantified at 4°C over a 30 days storage period. The stability in human plasma was also evaluated. Key findings Proteins expressed in SHuffle resulted in increased levels of protein expression and solubility. Low critical micelle concentration value and high micelle encapsulation efficiency (<200 nm) achieved via direct dissolution method. Anti-Aβ-loaded micelles were around 2.2-fold more stable than Anti-Aβ in plasma solution. A sustained in-vitro release of Anti-Aβ from micelles was observed. Conclusions Results confirmed that Pluronic-micelles pose benefits as a nano-carrier to increase the stability of Anti-Aβ scFvin in the plasma.