Protein immobilization on graphene oxide or reduced graphene oxide surface and their applications: Influence over activity, structural and thermal stability of protein

Due to the essential role of biological macromolecules in our daily life; it is important to control the stability and activity of such macromolecules. Therefore, the most promising route for enhancement in stability and activity is immobilizing proteins on different support materials. Furthermore, large surface area and surface functional groups are the important features that are required for a better support system. These features of graphene oxide (GO) and reduced graphene oxide (RGO) makes them ideal support materials for protein immobilization. Studies show the successful formation of GO/RGO-protein complexes with enhancement in structural/thermal stability due to various interactions at the nano-bio interface and their utilization in various functional applications. The present review focuses on protein immobilization using GO/RGO as solid support materials. Moreover, we also emphasized on basic underlying mechanism and interactions (hydrophilic, hydrophobic, electrostatic, local protein-protein, hydrogen bonding and van der Walls) between protein and GO/RGO which influences structural stability and activity of enzymes/proteins. Furthermore, GO/RGO-protein complexes are utilized in various applications such as biosensors, bioimaging and theranostic agent, targeted drug delivery agents, and nanovectors for drug and protein delivery. (C) 2021 Elsevier B.V. All rights reserved.