In this study, nanofibers containing an amyloid-like bovine serum albumin (AL-BSA) carrier and a model drug (ampicillin) were produced by electrospinning. The release behavior of ampicillin was compared from electrospun nanofibers prepared as either coaxial or single-needle types. SEM images showed that the membranes had a uniform and smooth structure and the core/shell fibers were found to be thicker than the core fibers. Core/shell production was proved by transmission electron microscopy images. Fourier transform infrared spectroscopy indicated the existence of compatibility between ampicillin and the AL-BSA matrix. The in vitro antimicrobial properties of ampicillin were studied through the comparison of bacterial inhibition zones and ampicillin was found to be more effective against Gram-positive Staphylococcus aureus than Gram-negative Escherichia coli. Moreover, in vitro drug release tests were conducted to explore the relationship between the shell thickness and the drug release rate. A burst release was observed for all membranes owing to the small fiber diameters and thus short diffusion lengths. For core membranes, the drug release mechanism followed Fickian transport, which was close to zero-order kinetic. A typical biphasic release mechanism was observed for the core/shell nanofibers. Overall, we present the first evidence of AL-BSA as a potential core/shell drug mediator.
Keywords: Amyloid-like protein; Biphasic release; Coaxial electrospinning.
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