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Recent years have witnessed unprecedented increase in the use of nanoparticles in various sectors viz. electronics, catalysis, agriculture, textile, cosmetics, bio-medicine, packaging, house-holds and food-associated consumer products. This has led to the inevitable release of nanoparticles into the environment, which can have negative impact on living beings. Humans can also be exposed to these nanoparticles either intentionally or accidently. Nanoparticles can enter in the human body through food chain, inhalation, open wounds, drugs and intravenous injections etc. In majority of these cases, the nanoparticles may pass through the various cell layers, cell sap and finally enter into the blood. Upon interaction with biological fluid, nanoparticles come in close proximity particularly to the proteins present in the fluid. The assembly of proteins surrounding the nanoparticle's surface is called as protein corona and their complex is known as protein-nanoparticle complex. Formation of protein corona is a vibrant and driving process, which plays a pivotal role in the functioning of nanoparticles in biological systems. Moreover, due to interaction of proteins with nanoparticles, conformational changes may occur in the native structure of protein, which may lead to change in the functioning of proteins towards its cellular interaction. The present review provides in-depth knowledge about the formation of protein corona around nanoparticles and the factors regulating this process. Further, it discusses various techniques that can be used for the protein corona analysis and obtaining information about molecular consequences upon nanoparticle's exposure. Finally, the functional aspects of protein-nanoparticle complex have been discussed in detail. In-depth understanding of protein-nanoparticles complex can be instrumental to generate well-suited nanoparticles with desired surface characteristics in the way to biological application.

Styrene is a nonpolar organic compound used in very high volume for the industrial scale production of commercially important polymers such as polystyrene resins as well as copolymers like acrylonitrile butadiene styrene, latex, and rubber. These resins are widely used in the manufacturing of various products including single‐use plastics such as disposable cups and containers, protective packaging, heat insulation, and so forth. The large‐scale utilization leads to the over‐accumulation of styrene waste in the environment causing deleterious health risks including cancer, neurological impairment, dysbiosis of central nervous system, and respiratory problems. To eliminate the accumulating waste. Microbial enzyme‐based system represents the most environmental friendly and sustainable approach for elimination of styrene waste. However, comprehensive understanding of the enzyme–substrate interaction and associated pathways would be crucial for developing large‐scale disposal systems. This study aims to understand the molecular interaction between the protein‐ligand complexes of the styrene catabolic reactions by bacterial enzymes of sty operon. Molecular docking analysis for catalytic enzymes namely, styrene monooxygenase (SMO), styrene oxide isomerase (SOI), and phenylacetaldehyde dehydrogenase (PAD) of the bacterial sty operon was carried out with their individual substrates, that is, styrene, styrene oxide, and phenylacetic acid, respectively. The binding energy, amino acids forming binding cavity, and binding interactions between the protein‐ligand binding sites were calculated for each case. The obtained binding energies showed a stable association of these complexes indicating the future scope of their utilization for large‐scale bioremediation of styrene, and its commercially used polymers and copolymers.

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