Bovine hemoglobin adsorption onto modified silica nanoparticles: Multi-spectroscopic measurements based on kinetics and protein conformation

Nanoparticle Effects on Stress Response Pathways and Nanoparticle–Protein Interactions

“…A follow-on study found similar observations using human Hb, and it was determined that the increased oxygen affinity was due to changes in the structure of the Hb proteins and interaction with the Si NPs [ 394 ]. Adsorption of bovine Hb to Si NPs induced structural changes and heme degradation, where hydrophobic Si NPs were found to induce a greater change than hydrophilic Si NPs [ 395 ]. Hydrophobic interactions were found to be involved in the adsorption of human Hb to SiO 2 NPs, and temperature affected the binding affinity of the NPs to the Hb [ 360 ].…”

Biomolecular Corona Associated with Nanostructures: The Potentially Disruptive Role of Raman Microscopy

“…Finally, FTIR has also been used as a technique to investigate BC phenomena. Some examples include the characterization of BCs associated with silver/gold nanoalloy, [ 28 ] the characterization of proteins associated with iron oxide magnetic NPs and SPIONs, [ 16,24 ] and the analysis of the interaction between BHb and silica NPs, [ 22 ] of blood‐derived BCs on the surface of 2D model nanosheet structures of molybdenum disulfide (MoS 2 ), [ 6 ] of protein association on the surface of gold nanostructures with different shapes, and of PC formation on the surface of polyacrylic acid‐coated cobalt ferrite NPs (PAA NPs) and silica NPs. [ 134 ]…”

“…[ 5 ] UV–vis spectra analysis can also be used to analyze the effect of the formation of BCs on the structure of the proteins associated with the nanostructure, such as in the study by Yang et al., where the structural changes induced on bovine hemoglobin (BHb) upon exposure to hydrophilic and hydrophobic silica NPs were analyzed through UV–vis spectroscopy. [ 22 ] Fluorescence spectroscopy is also commonly used to analyze BC and nanostructure–protein interactions. For example, the endogenous fluorescence of proteins can be used to track their binding to nanostructures.…”

“…A wide range of techniques have been used in BC studies, such as dynamic light scattering (DLS), [ 9 ] sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), mass spectrometry (MS)‐based approaches, [ 10–21 ] UV/vis spectroscopy, Fourier‐transform infrared spectroscopy (FTIR), [ 22 ] atomic force microscopy (AFM), [ 23 ] scanning electron microscopy (SEM), [ 24–27 ] transmission electronic microscopy (TEM), [ 23 ] and circular dichroism spectroscopy (CD). [ 28 ] Various information (size, surface properties, morphology, structure, etc.)…”

“…[5,6] However, BCs can be exploited or even altered, in order to be made beneficial for targeting purposes as they can enable specific cells to more easily recognize NPs and may lead to a reduction in their toxicity. [7,8] A wide range of techniques have been used in BC studies, such as dynamic light scattering (DLS), [9] sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), mass spectrometry (MS)-based approaches, [10][11][12][13][14][15][16][17][18][19][20][21] UV/vis spectroscopy, Fourier-transform infrared spectroscopy (FTIR), [22] atomic force microscopy (AFM), [23] scanning electron microscopy (SEM), [24][25][26][27] transmission electronic microscopy (TEM), [23] and circular dichroism spectroscopy (CD). [28] Various information (size, surface properties, morphology, structure, etc.)…”