LAUSR

Abstract Herein, we report the biochemical interaction between copper-oxide nanoparticles (CuO NPs) and vital biomolecules viz., deoxyribonucleic acid (DNA) and vital proteins such as bovine serum albumin (BSA), human serum albumin (HSA) and collagen in presence of various types of surfactants (non-ionic, cationic and anionic surfactants). Bare CuO NPs are synthesized by wet chemical method and were characterized by X-ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscopy (SEM), UV–vis spectroscopy and Energy Dispersive X-ray Spectroscopy (EDAX) studies. The interaction study of CuO NPs-protein was done using dynamic light scattering studies, fluorescence spectroscopy, UV–vis spectroscopy, circular dichroism technique and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The spectroscopic evaluation clarifies various features of binding through the molecular interactions of CuO NPs and serum proteins along with surfactants. Gel electrophoresis was used to study NPs-DNA interactions in the presence and absence of surfactants. Nanoparticle-protein binding was found to be strongest in CTAB, SDS and Tween 80 based systems. Tween 80 surfactant was also found to provide continual biocompatibility to CuO NPs. The study gives detail information about the effect of different surfactant coatings on CuO nanoparticle surfaces along with their effects on vital biomolecules. The findings will thus be very helpful in designing stable CuO NP formulations for biomedical applications.