Interfacing proteins with graphitic nanomaterials: from spontaneous attraction to tailored assemblies

Abstract

This critical review aims at giving insights on the spontaneous tendency of proteins and their constitutive parts to adsorb on graphitic nanomaterials (GNMs) through non-covalent interactions occurring at their interfaces. Specifically, it focuses on the theoretical and experimental studies carried out to comprehend in depth the forces ruling the adsorption processes of proteins on fullerene, carbon nanotubes and graphene. In a systematic way the reader is guided through the most recent and representative examples describing at the atomistic level of detail the structural modalities and the chemico-physical principles through which amino acids, polypeptides and folded proteins interact with GNMs' surface, thereby taking into consideration the mutual effects of both protein structural complexity and nanomaterial topology. Based on their chemical and structural features, the study and understanding of the protein-nanomaterial interfaces can be exploited in the view of design and control the spontaneous formation of biologically-active hybrid materials for the development of new tailored applications in the field of sensing, nanomedicine and biochemistry.

Targeting G Protein‐Coupled Receptors with Magnetic Carbon Nanotubes: The Case of the A3 Adenosine Receptor

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The Enigma of Amyloid Forming Proteins: Insights From Molecular Simulations

“…[63] Several reviews summarise the plethora of research describing the common modes in which nanostructured materials interact with biological molecules such as membranes, DNA, and peptides/proteins, and, within our current focus, their possible role in protein aggregation. [64][65][66][67][68] Despite the extensive number of studies in this field there is still a lot to learn about nanomaterial interactions with biological matter. Specifically in relation to amyloid formation, nanomaterials may inhibit or promote cytotoxicity at three different stages of the fibrillation process: (1) by disruption of the nucleation phase, i.e.…”

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Patterning Porous Networks through Self‐Assembly of Programmed Biomacromolecules

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