Theranostic potential of gold nanoparticle-protein agglomerates

Abstract

Owing to the ever-increasing applications, glittered with astonishing success of gold nanoparticles (Au NPs) in biomedical research as diagnostic and therapeutic agents, the study of Au NP-protein interaction seems critical for maximizing their theranostic efficiency, and thus demands comprehensive understanding. The mutual interaction of Au NPs and proteins at physiological conditions may result in the aggregation of protein, which can ultimately lead to the formation of Au NP-protein agglomerates. In the present article, we try to appreciate the plausible steps involved in the Au NP-induced aggregation of proteins and also the importance of the proteins' three-dimensional structures in the process. The Au NP-protein agglomerates can potentially be exploited for efficient loading and subsequent release of various therapeutically important molecules, including anticancer drugs, with the unique opportunity of incorporating hydrophilic as well as hydrophobic drugs in the same nanocarrier system. Moreover, the Au NP-protein agglomerates can act as 'self-diagnostic' systems, allowing investigation of the conformational state of the associated protein(s) as well as the protein-protein or protein-Au NP interaction within the agglomerates. Furthermore, the potential of these Au NP-protein agglomerates as a novel platform for multifunctional theranostic application along with exciting future-possibilities is highlighted here.

Bio-identity and fate of albumin-coated SPIONs evaluated in cells and by the C. elegans model

“…[12] Aggregates of iron oxide NPs increase cell uptake and enhance cell contrast in magnetic resonance imaging (MRI) without compromising cell viability. [13] Protein-nanoparticle aggregates were proposed as biocompatible drug carriers [14] and their use was suggested to increase the cell viability of some nanomaterials. [15,16] However, adsorption of proteins by NPs in an uncontrolled and non-reproducible manner will have limited applications in nanomedicine.…”

Self‐Assembling Proteins for Design of Anticancer Nanodrugs

“…Nanoparticle-induced self-assembly of proteins is versatile for the formation of various nanostructures, including nanoparticles with an inorganic core and a protein shell, protein nanoparticles with embedded inorganic nanoparticles, and protein fibrils. [72] The formation of nanostructures consequently brings about conformational change in the higher order structures of proteins. [73] The formed nanostructures combine the properties and advantages of inorganic nanoparticles and proteins and are applicable in loading of hydrophobic drugs.…”

“…In order to minimize the side effects of the uncontrollable formation of the protein corona in blood, self‐assembly of proteins and nanoparticles in solutions has been investigated as a strategy to construct nanodrugs with improved therapeutic efficiencies. Nanoparticle‐induced self‐assembly of proteins is versatile for the formation of various nanostructures, including nanoparticles with an inorganic core and a protein shell, protein nanoparticles with embedded inorganic nanoparticles, and protein fibrils . The formation of nanostructures consequently brings about conformational change in the higher order structures of proteins .…”

Anisotropic Gold Nanoparticle-Cell Interactions Mediated by Collagen

“…This is also well described in the recent idea of protein corona formation when nanoparticles are exposed to biological fluids [12]. Moreover, by having a protein as a layer on top of the nanoparticles, the options for further applications expands [13]. Proteins are a good source of different functional groups that can serve as binding sites for other molecules such as dyes, antibodies or drugs [14].…”