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