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

Abstract

Herein, the effects of bovine hemoglobin (BHb) binding to hydrophilic silica nanoparticles (SN1) and hydrophobic silica nanoparticles (SN2) were explored under physiological conditions. SEM and XRD were used to characterize silica nanoparticles (SNs). Zeta potential and DLS confirmed the formation of protein corona (PC), and SN2 showed more increase in their size after PC formation comparing with SN1. The adsorption isotherms were fitted well by the Freundlich model, and the kinetics tended to follow pseudo-second-order kinetics. Then, the second structure of BHb has been analyzed by UV–vis and FT-IR spectroscopy, which implied the impact of SN2 on the secondary structure of BHb was greater than that of SN1 on BHb. Moreover, fluorescence spectroscopy and Raman spectroscopy showed that SNs may induce heme degradation to form fluorescent heme product, resulting in increased fluorescence intensity. This investigation will be significant in exploring the toxicity profile of SNs for their in vivo.