Nanotechnologies have garnered significant attention in the scientific community due to their applications in various areas of medicine. In particular, silvernanoparticles(Ag-NPs) are noteworthy for their antibacterial and surface plasmonic properties, which depend on their shape anisotropy. Understanding the interactions of Ag-NPs with biomolecules in biological systems is essential for the safe use of new treatments involving these materials. For this reason, we study serum albumin(BSA), the most abundant protein in blood, which plays key roles such as regulating pH, solubilizing certain drugs, and transporting pharmaceutical agents. Examining the behavior of nanoparticles with albumin (Ag-NPs/BSA) can provide valuable insights into their pharmacological effects.[1]

In this work, we've confirmed that the presence of prism-shapedAg-NPs and sphericalAg-NPs induces changes in the protein structure, that include aggregation. The technologies used include FourierTransformInfraredSpectroscopy(FT-IR), Small-AngleX-RayScattering(SAXS), and Transmission Electron Microscopy(TEM) to study these interactions

FTIR results have shown slight differences between the BSA spectrum and the Ag-NPs spectrum in band shape, indicating minimal interaction. In contrast, XAS results have revealed strong attractive interactions leading to aggregation. Finally, TEM confirmed the aggregation of nanoparticles in the presence of BSA. [2]

[1] http://dx.doi.org/10.1016/j.molliq.2016.02.103

[2] http://dx.doi.org/10.1016/j.cbi.2016.05.018