Gold nanoprisms possess remarkable optical properties that make them useful for medical biotechnology applications such as diagnosis and photothermal therapy. However, shape-selective synthesis of gold nanoprisms is not trivial and typically requires either toxic surfactants or time-consuming purification protocols, which can limit their applicability. Here, we show how triangular gold nanoprisms of different sizes can be purified by precipitation using the non-toxic glutathione ligand, thereby removing the need for toxic surfactants and bottleneck purification techniques. The protocol is amenable for direct scaling up as no instrumentation is required in the critical purification step. The new purification method provides a two-fold increased yield in gold nanoprisms compared to electrophoretic filtration, while providing nanoprisms of similar localized surface plasmon resonance wavelength. Crucially, the gold nanoprisms isolated using this methodology show fewer non-specific interactions with cells and lower cellular internalization, which paves the way for a higher selectivity in therapeutic applications.
Several nitrogen-containing graphene-derived materials have been obtained using DBU and DMF as nitrogen sources, and further employed as heterogeneous catalysts.
Exposure of nanomaterials (NMs) to biological medium results in their direct interaction with biomolecules and the formation of a dynamic biomolecular layer known as the biomolecular corona. Despite numerous published data on nano-biointeractions, the role of protein glycosylation in the formation, characteristics, and fate of such nano-biocomplexes has been almost completely neglected, although most serum proteins are glycosylated. This study aimed to systematically investigate the differences in interaction of metallic NPs with glycosylated vs nonglycosylated transferrin. To reach this aim, we compared interaction mechanisms between differently sized, shaped, and surface-functionalized silver NMs and gold NMs to commercially available human transferrin (TRF), a glycosylated protein, and to its nonglycosylated recombinant form (ngTRF). Bovine serum albumin (BSA) was also included in the study for comparative purposes. Characterization of NMs was performed using transmission electron microscopy and dynamic and electrophoretic light scattering techniques. Fluorescence quenching and circular dichroism methods were used to evaluate protein binding constants on the nanosurface and conformational changes after the protein–NM interactions, respectively. Competitive binding of TRF, ngTRF, and BSA to the surface of different NMs was evaluated by separating them after extraction from protein corona by gel electrophoresis following quantification with a commercial protein assay. The results showed that the binding strength between NMs and transferrin and the changes in the secondary protein structure largely depend not only on NM physicochemical properties but also on the protein glycosylation status. Data gained by this study highlight the relevance of protein glycosylation for all future design, development, and efficacy and safety assessment of NMs.