Abstract

Graphene oxide nanoribbons with superior physicochemical properties acquired from graphene and carbon nanotubes have been used in various applications including biomedical applications. For biomedical applications, it is of utmost importance to understand how these graphene oxide nanoribbons interact with proteins and the influence they have on protein conformation and function. In this regard, an attempt has been made to evaluate the utility of graphene oxide nanoribbons as a compatible biomaterial for lysozyme (Lys) protein. In this study, graphene oxide nanoribbons (GONRs) synthesized from multiwalled carbon nanotubes (MWCNTs) were first functionalized with (3-aminopropyl)triethoxysilane (APTES) and further modified with vanillin (Val) to obtain Val-APTES-GONRs. On characterization, it was found that the Val-APTES-GONRs material had a ribbonlike morphology with abundant functionalities for interaction with protein. On evaluation of Val-APTES-GONRs as a compatible biomaterial for Lys, studies revealed that a lower concentration of the as-synthesized material has less influence on the conformation and the structure of Lys with better activity, whereas higher concentrations of the as-synthesized material had a greater influence on conformation and the structure of Lys with decreased activity. Overall, the thermal stability of Lys was maintained after introducing the Val-APTES-GONRs material. In addition, transmission electron microscopy (TEM), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) and Raman spectroscopies were performed for Lys composites with Val-APTES-GONRs for further understanding biomolecular interactions. This study is beneficial for designing advanced graphene-based materials for numerous bioinspired applications and better biomaterials for biotechnological use.

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