Abstract We report an efficient approach for the fabrication of hydrophobic drug-loaded human serum albumin nanofibers for the first time. The successful formation of nanofibers was found closely related to… Click to show full abstract
Abstract We report an efficient approach for the fabrication of hydrophobic drug-loaded human serum albumin nanofibers for the first time. The successful formation of nanofibers was found closely related to the glutathione (GSH) concentration, solution temperature, and heating time. As-fabricated nanofibers were characterized by electron microscopy, Fourier transform infrared spectroscopy (FTIR) and X-ray powder diffraction (XRD). The electron micrographs show that nanofibers have cylindrical morphology and diameters of 70–120 nm and lengths of up to few micrometers with a smooth surface. GSH was found to contribute to the quicker unfolding of the HSA under high temperature (80–85 °C) which resulted in the strong interaction with paclitaxel, leading to a morphological transformation from nanoparticles to nanofibers. In addition, the possible mechanisms of nanofiber formation have been discussed.
               
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