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Investigation and control of protein adsorption for fluorescent nanosilver reference material
(2017)
Upon interaction of nanomaterials like noble metal nanoparticles (NPs) with biological systems like body fluids such as serum, a protein corona is formed.[1] This reversibly bound layer of proteins controls the transport of the NPs and their subsequent interaction with biological components.[2] The plasmonic properties of nobel metal NPs like Au and Ag can considerably affect the fluorescence properties of fluorophores in their vicinity, i.e., within a near field distance. Depending on the chemical composition, size and shape of these noble metal NPs, the spectral properties of the dye, and the particle-fluorophore distance, the fluorescence is quenched or in some cases enhanced.[3,4,5] This can be monitored by fluorescence intensity and lifetime measurements, with the latter effect being accompanied by an increase in fluorescence intensity and reduction in fluorescence lifetime due to an increase in radaiative rate constant. We utilized these effects to study and manipulate noble metal NP-protein interaction exemplarily for fluorophore-labeled bovine serum albumin (BSA) modified e.g. by succinylation, amination and the introduction of thiol groups, resulting in different binding affinities of the proteins.[6] Our results show that the fluorescent corona allows monitoring of the interaction of our accordingly protein-functionalized particles with biological model systems like solutions containing different amounts of various proteins. This can be eventually used for further in vitro and in vivo studies to assess the uptake, digestion, and excretion of surface functionalized noble metal NPs.