Abstract
Protein interactions with engineered gold nanoparticles (AuNPs) and the consequent formation of the protein corona are very relevant and poorly understood biological phenomena. The nanoparticle coverage affects protein binding modalities, and the adsorbed protein sites influence interactions with other macromolecules and cells. Here, we studied four common blood proteins, i.e., hemoglobin, serum albumin, α1-antiproteinase, and complement C3, interacting with AuNPs covered by hydrophobic 11-mercapto-1-undecanesulfonate (MUS). We use Molecular Dynamics and the Martini coarse−grained model to gain quantitative insight into the kinetics of the interaction, the physico-chemical characteristics of the binding site, and the nanoparticle adsorption capacity. Results show that proteins bind to MUS−capped AuNPs through strong hydrophobic interactions and that they adapt to the AuNP surfaces to maximize the contact surface, but no dramatic change in the secondary structure of the proteins is observed. We suggest a new method to calculate the maximum adsorption capacity of capped AuNPs based on the effective surface covered by each protein, which better represents the realistic behavior of these systems.
Highlights
Engineered nanoparticles (NPs) gained the attention of several branches of science due to their unique physical, chemical, and electrical properties, and they have been used in several emerging applications, such as biomedicine and catalysis [1,2]
The results show that hydrophobic interactions play the most relevant role in the AuNP–protein binding, and we propose a new methodology to evaluate the maximum adsorption capacity of NPs by means of classical Molecular Dynamics (MD) simulations
Most of the contact of the proteins with the all-MUS AuNP were achieved by hydrophobic amino acids, while the percentage of positively and negatively charged amino acids was quite low and depended on the binding site of the protein
Summary
Engineered nanoparticles (NPs) gained the attention of several branches of science due to their unique physical, chemical, and electrical properties, and they have been used in several emerging applications, such as biomedicine and catalysis [1,2]. The understanding of the interactions of NPs with the biological medium will help to design newer and safer nanomaterials with reduced toxicity and to develop nanomedicine applications such as drug delivery to well-defined biological sites [2,4]. The main problem in developing non-toxic and effective nanomaterials is caused by the lack of knowledge regarding nanoparticle interactions with the biological medium. It is well-known that when a NP comes in contact with a physiological environment such as blood, proteins and macromolecules readily interact and adsorb over the NP surface, creating a layer of biomolecules called the “corona” [5,6].
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