Amir Arasteh; Zolfaghar Lotfi; Mohammad Fazilat; Habibollah Nazem
Volume 6, Issue 2 , December 2017, , Pages 127-137
Abstract
Amyloid fibrils are a class of protein nanoparticles in which native proteins are converted into dense fibers. The aggregation can be pathogenic or non-pathogenic. Recently, these fibrils have been considered for the production of Bio–nanomaterials due to their unique structure. In this study, ...
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Amyloid fibrils are a class of protein nanoparticles in which native proteins are converted into dense fibers. The aggregation can be pathogenic or non-pathogenic. Recently, these fibrils have been considered for the production of Bio–nanomaterials due to their unique structure. In this study, Bovine serum albumin was used as a model protein to optimize the fibrillation process. Concentrations of 2-10 mg/ml were prepared in buffer at different pH values of 3-7 and placed at 0-70 ºC for 0 to 48 hours, and the amounts of produced amyloid fibrils were analyzed by spectrophotometry, fluorimetry and circular dichroism. The spectra obtained from the Congo red absorption method were compared on the basis of the maximum wavelength and absorption at maximum wavelengths with a sample containing Congo red. The concentration of 10 mg/ml of protein, which was 48 hours in buffer at pH = 4 at 50 ºC, produced the highest amounts of amyloid. Optimum conditions were obtained by ThT fluorescence and circular dichroism at a concentration of 10 mg/ml, pH = 4, 70 ºC and 48 hours. The presence of the fibers was confirmed by transmission electron microscope images. The insoluble structure and dimensions of amyloid fibrils can be describe them as new Bio–nanomaterials. Optimizing the production of these structures allows them to be produced at higher scales.
