Interactions Between Plasmonic Nanostructures and Proteins

In the development of a nanodevice for biomedical applications, the study of the interactions with the biomolecules is essential. Proteins, in particular, are known to be easily adsorbed on the surface of the nanoparticles and the resulting complex is the one that will be effectively internalized by the target cells. Owing to the versatility of the preparation methods available and the unique optical properties, gold nanomaterials represent an excellent choice to study this interaction. This chapter will initially describe the synthesis of gold nanorods and nanoshells that are able to absorb light in the near-infrared (NIR) region. Then, the methods available for the function‐ alization of their surface will be discussed. The surface plasmon absorption will be used as an optical tool to monitor the process of preparation and surface modifica‐ tion. In the last section of the chapter, fluorescence and microscopy techniques will be used to follow the formation and characterize the protein-nanoparticle complex. The modifications of the emission spectra of two model proteins, bovine serum albumin (BSA) and myoglobin (Mb), will be analyzed in detail. The data will demonstrate that structural rearrangements following the adsorption on the surface of the nanoparticles are responsible for the changes in the fluorescence of the tryptophan residues of the protein. The data will be discussed in terms of static and dynamic quenching, proving the formation of a protein-nanoparticle complex. Atomic force microscopy (AFM) measurements will allow the direct visualization of this complex.