The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

Abstract

Interactions between differently functionalised silver and gold nanoparticles (NPs) as well as polystyrene nanoparticles with bovine serum albumin (BSA) are studied using circular dichroism (CD) spectroscopy. It is found that the addition of NPs to the protein solution destroys part of the helical secondary structure of the protein as a result of surface adsorption. From the loss of free protein and hence the extent of their structural change adsorption equilibrium constants are derived. The results reveal that citrate‐coated gold and silver NPs exhibit much stronger interactions with BSA than polymeric or polymer‐coated metallic NPs. It is therefore concluded that for the particles considered, the influence of surface composition on the interaction behaviour dominates that of the core.

New views on cellular uptake and trafficking of manufactured nanoparticles

“…A layer of proteins forms on the NP surfaces, the so-called protein corona [10,[31][32][33][34][35][36][37][38][39][40][41][42][43]. Consequently, cell surface receptors, which activate the endocytosis machinery, actually encounter NPs enshrouded in biomolecules rather than bare particles.…”

Influence of individual ionic components on the agglomeration kinetics of silver nanoparticles

“…Numerous toxicological studies have revealed that nanoparticles are much more reactive and toxic than larger particles made from the same material [6][7][8][9][10]. It is therefore of paramount interest to characterize NP suspensions in salt-containing environments and to ultimately also assess the influence of biomolecules on their behavior [11].…”

Blood protein and blood cell interactions with gold nanoparticles: the need for in vivo studies

“…Despite this, it is possible that proteins do denature or unfold upon binding or adsorbing to NPs [24,25]. For instance, using albumin alone Treuell et al found that the α -helical structures of albumin are destroyed in the presence of 20 nm citrated gold and silver NPs while it does not with polymeric NPs [24].…”

“…For instance, using albumin alone Treuell et al found that the α -helical structures of albumin are destroyed in the presence of 20 nm citrated gold and silver NPs while it does not with polymeric NPs [24]. Zhang and colleagues also demonstrated aggregate formation with DLS, TEM and fluorescence microscopy in the lysozyme solution when incubated with GNPs (90 nm citrate stabilized) [25].…”