Morphological Effects of CuO Nanostructures on Fibrillation of Human Serum Albumin

The influence of different morphologies of nanostructures on amyloid fibrillation has been investigated by monitoring the fibrillation of human serum albumin (HSA) in the presence of rod-, sphere-, flower-, and star-shaped copper oxide (CuO) nanostructures. The different morphologies of CuO have been synthesized from an aqueous solution-based precipitation method using various organic acids, viz., acetic acid, citric acid, and tartaric acid. The fibrillation process of HSA has been examined using various biophysical techniques, e.g., Thioflavin T fluorescence, Congo red binding studies through UV spectroscopy, circular dichroism spectroscopy, and fluorescence microscopy. The monolayer protein coverage on the CuO nanostructures has been established through DLS studies, and the well-fitted Langmuir isotherm model has been used to interpret the differential adsorption behavior of HSA molecules on the CuO nanostructures. The nanostar-shaped CuO, by virtue of their higher specific surface area (94.45 m(2) g(1)), presence of high indexed facets {211} and high positive surface charge potential (+16.2 mV at pH 7.0) was found to show the highest adsorption of the HSA monomers and thus was more competent to inhibit the formation of HSA fibrils compared to the other nanostructures of CuO