Protein Nanomaterial Interactions Structural And Dynamic Aspects

Abstract

Owing to their unique properties, the noble metallic nanoparticles and graphenic nanomaterials find their applications in diverse fields of science. Particularly in the field of biomedicine, nanomaterials are being used in drug delivery, tumor targeting, bio-sensing, tissue engineering and photo thermal therapy. The accidental or the intentional exposure of human body towards these nanomaterials paves their way into the body. But at the same time, the knowledge about the exposure risks and the biocompatibility of these nanomaterials remains largely unknown. Some of the studies have found that the nanomaterials show adverse effects towards the biological systems under in vitro and in vivo conditions. When these nanomaterials come in contact with biomolecules, such as peptides and proteins, layers of biomolecules cover their surfaces, leading to the formation of a dynamic and competitive protein corona. The formation of protein corona has the potential to affect the properties of both the nanoparticles (e.g., cellular uptake, accumulation, degradation and clearance from the body) and the protein adsorbed on the surface (e.g., protein conformation and function). Hence, unexpected biological responses and toxicity may be induced. It therefore becomes important to probe the nature of interactions of biomolecules at their individual residual level with nanomaterials. Depending upon the surface charges of both; the nanomaterials and the proteins, there may either be strong and irreversible or weaker and reversible interactions between proteins and nanomaterials involving electrostatic or covalent interactions. Thus, the understanding of such protein-nanomaterial interactions can be exploited for the generation of the safe and biocompatible nanomaterials with optimized surface properties in a biological milieu. The main aim of our work is to probe into the residual level conformational changes in the proteins in presence of nanomaterials and the dynamic aspects of such interactions. Using two-dimensional NMR spectrosc...