Protein corona formation of human serum albumin with carbon quantum dots from roast salmon†
When food-borne nanoparticles enter biological systems, they can interact with various proteins to form protein coronas, which can affect their physicochemical properties and biological identity. In this study, the protein corona formation of carbon quantum dots (CQDs) from roast salmon with human serum albumin (HSA) was explored. Furthermore, the biological identity of the HSA-CQD coronas, in relation to cell apoptosis, energy, glucose and lipid metabolism and acute toxicity in mice, was also investigated. The HSA-CQD coronas were formed between HSA and CQDs via a static binding mechanism, and the binding site of CQDs on HSA was located at both Sudlow's site I and site II. After entering the cytoplasm, the HSA-CQD coronas became localized in the lysosomes and autolysosomes. Importantly, the HSA coronas reduced the cytotoxicity of the CQDs from 18.65% to 9.26%, and the energy metabolism was rectified by changing from glycolytic to aerobic metabolism. The glucose and lipid metabolite profile of cells exposed to the HSA-CQD coronas differed from that of those treated with CQDs, indicating that the HSA-CQD coronas rectified metabolic disturbances caused by CQDs. Histopathological and blood biochemical analysis revealed no statistically significant differences between the treated and control mice after a single CQDs dose of 2000 mg per kg body weight. Overall, the results confirmed the formation of protein coronas between HSA and food-borne fluorescent CQDs, and could be helpful for evaluating the safety of fluorescent CQDs in cooked food items.