Structure and Function of Enzymes Adsorbed onto Single-Walled Carbon Nanotubes

Karajanagi, Sandeep S.; Vertegel, Alexey; Kane, Ravi S.; Dordick, Jonathan S.

doi:10.1021/la047994h

Cited by 483 publications

(462 citation statements)

References 30 publications

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“…They demonstrated that a strong π -π interaction existed between the individual hexagonal cells of the GO basal planes and the glucose oxidase. This is similar to the interactions between the protein molecules and CNTs where the π -π stacking interaction is a dominated factor [112,120] . Apparently, the enzyme immobilization onto GO might be a result of the synergic effect of the different interactions.…”

Section: Noncovalent Adsorption Of the Protein/ Enzyme Molecules On Tsupporting

confidence: 56%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

208

107

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This review selectively describes the recent progress in the interactions of proteins (enzymes) and shortchain peptides with graphene and graphene oxide (GO). Particularly, the advances of the immobilization mechanisms of enzymes on graphene and GO, the catalytic properties of the immobilized enzymes, and their applications are summarized in detail. The interfacings of the peptides with graphene and GO, the as assembled conjugates, and their potential applications are discussed briefly. The possible ongoing development for the assembly of conjugates of graphene and GO with proteins and peptides in a controlled manner is speculated upon.

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Section: Noncovalent Adsorption Of the Protein/ Enzyme Molecules On Tsupporting

confidence: 56%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

208

107

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“…Experimental measurements of the thermodynamics of protein folding have been performed primarily in bulk water (41). Although many experiments have probed how interfaces affect protein folding, structure, and function (29,42), to the best of our knowledge, there are no temperature-dependent thermodynamic measurements of self-assembly at interfaces. Extensions of atomic force microscope experiments of pulling a hydrophobic polymer attached to a surface (43) have the potential to quantify the thermodynamics of hydrophobic interactions in interfacial environments described here.…”

Section: Modelsmentioning

confidence: 99%

Extended surfaces modulate hydrophobic interactions of neighboring solutes

Patel

Varilly

Jamadagni

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

157

224

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Interfaces are a most common motif in complex systems. To understand how the presence of interfaces affects hydrophobic phenomena, we use molecular simulations and theory to study hydration of solutes at interfaces. The solutes range in size from subnanometer to a few nanometers. The interfaces are self-assembled monolayers with a range of chemistries, from hydrophilic to hydrophobic. We show that the driving force for assembly in the vicinity of a hydrophobic surface is weaker than that in bulk water and decreases with increasing temperature, in contrast to that in the bulk. We explain these distinct features in terms of an interplay between interfacial fluctuations and excluded volume effects-the physics encoded in Lum-Chandler-Weeks theory [Lum K, Chandler D, Weeks JD (1999) J Phys Chem B 103:4570-4577]. Our results suggest a catalytic role for hydrophobic interfaces in the unfolding of proteins, for example, in the interior of chaperonins and in amyloid formation. binding | hydrophobicity | thermodynamics H ydrophobic effects are ubiquitous and often the most significant forces of self-assembly and stability of nanoscale structures in liquid matter, from phenomena as simple as micelle formation to those as complex as protein folding and aggregation (1, 2). These effects depend importantly on length scale (3-5). Water molecules near small hydrophobic solutes do not sacrifice hydrogen bonds, but have fewer ways in which to form them, leading to a large negative entropy of hydration. In contrast, hydrogen bonds are broken in the hydration of large solutes, resulting in an enthalpic penalty. For hydrophobic solutes in bulk water at standard conditions, the cross-over from one regime to the other occurs at around 1 nm (3-6) and marks a change in the scaling of the solvation free energy from being linear with solute volume to being linear with exposed surface area. In bulk water, this crossover provides a framework for understanding the assembly of small species into a large aggregate.Typical biological systems contain a high density of interfaces, including those of membranes and proteins, spanning the entire spectrum from hydrophilic to hydrophobic. Whereas water near hydrophilic surfaces is bulk-like in many respects, water near hydrophobic surfaces is different, akin to that near a liquid-vapor interface (3-5, 7-9). Here, we consider how these interfaces alter hydrophobic effects. Specifically, to shed light on the thermodynamics of hydration at, binding to, and assembly at interfaces, we study solutes with a range of sizes at various self-assembled monolayer interfaces over a range of temperatures using molecular simulations and theory.Our principal results are that, although the hydration thermodynamics of hydrophobic solutes at hydrophilic surfaces is similar to that in bulk, changing from entropic to enthalpic with increasing solute size, it is enthalpic for solutes of all length scales near hydrophobic surfaces. Further, the driving force for hydrophobically driven assembly in the vicinity of hydrophobic ...

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“…80 An alternative bioconjugation strategy that offers more control over protein orientation while circumventing the structural perturbation caused by direct adsorption is the hybrid noncovalent/covalent approach (Figure 1b, c). In one approach, the SWCNT is noncovalently covered by a synthetic or biological polymer that is covalently conjugated to the protein (Figure 1b).…”

Section: Hybrid Approach: Covalent Attachment Tomentioning

confidence: 99%

“…80,100 The fewer degrees of freedom available to an adsorbed protein, combined with suboptimal orientation or adsorption-induced conformational alterations, may result in loss of protein specificity or activity. 80 The use of natural membrane fragments for suspending SWCNTs offers a much more direct approach to immobilizing membrane proteins, circumventing the need to reconstitute a synthetic membrane and benefiting from an inherent protein environment that has been optimized by nature. However, as is the case with purified protein adsorption, one drawback of using natural membrane fragments is the heterogeneity of nonspecifically adsorbed complexes and nonuniform protein distribution.…”

Section: Engineering Rules For Biomolecule-swcntmentioning

confidence: 99%

Noncovalent Protein and Peptide Functionalization of Single-Walled Carbon Nanotubes for Biodelivery and Optical Sensing Applications

Antonucci

Kupis-Rozmysłowicz

Boghossian

2017

ACS Appl. Mater. Interfaces

176

161

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ABSTRACT:The exquisite structural and optical characteristics of single-walled carbon nanotubes (SWCNTs), combined with the tunable specificities of proteins and peptides, can be exploited to strongly benefit technologies with applications in fields ranging from biomedicine to industrial biocatalysis. The key to exploiting the synergism of these materials is designing protein/peptide-SWCNT conjugation schemes that preserve biomolecule activity while keeping the near-infrared optical and electronic properties of SWCNTs intact. Since sp 2 bondbreaking disrupts the optoelectronic properties of SWCNTs, noncovalent conjugation strategies are needed to interface biomolecules to the nanotube surface for optical biosensing and delivery applications. An underlying understanding of the forces contributing to protein and peptide interaction with the nanotube is thus necessary to identify the appropriate conjugation design rules for specific applications. This article explores the molecular interactions that govern the adsorption of peptides and proteins on SWCNT surfaces, elucidating contributions from individual amino acids as well as secondary and tertiary protein structure and conformation. Various noncovalent conjugation strategies for immobilizing peptides, homopolypeptides, and soluble and membrane proteins on SWCNT surfaces are presented, highlighting studies focused on developing near-infrared optical sensors and molecular scaffolds for self-assembly and biochemical analysis. The analysis presented herein suggests that though direct adsorption of proteins and peptides onto SWCNTs can be principally applied to drug and gene delivery, in vivo imaging and targeting, or cancer therapy, nondirect conjugation strategies using artificial or natural membranes, polymers, or linker molecules are often better suited for biosensing applications that require conservation of biomolecular functionality or precise control of the biomolecule's orientation. These design rules are intended to provide the reader with a rational approach to engineering biomolecule-SWCNT platforms, broadening the breadth and accessibility of both wild-type and engineered biomolecules for SWCNT-based applications.

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Structure and Function of Enzymes Adsorbed onto Single-Walled Carbon Nanotubes

Cited by 483 publications

References 30 publications

Interactions of graphene and graphene oxide with proteins and peptides

Interactions of graphene and graphene oxide with proteins and peptides

Extended surfaces modulate hydrophobic interactions of neighboring solutes

Noncovalent Protein and Peptide Functionalization of Single-Walled Carbon Nanotubes for Biodelivery and Optical Sensing Applications

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