Amino acid adsorption on single-walled carbon nanotubes

Roman, Tanglaw; Diño, Wilson Agerico; Nakanishi, Hiroshi; Kasai, Hideaki

doi:10.1140/epjd/e2006-00043-1

Cited by 69 publications

(57 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, the size and curvature of a nanoparticle may play a major role in the adsorption patterns of proteins not only due to geometric adaptation of the protein to a nanoparticle of similar size, but also due to changes in the physico-chemical properties of the nanoparticle itself. DFT calculations of amino acid adsorption on a single-walled carbon nanotube (SWCNT) showed that glycine adsorbs more strongly on a nanotube (3,3) than on a flat graphite surface, whereas phenylalanine adsorbs more strongly on a flat graphite surface, and the amino acids cysteine and histidine, showed no significant change in their adsorption energies (Roman et al 2006). Binding free energy calculations of amyloidogenic apoC-II(60-70) peptide on fullerene, CNT and graphene using MD simulations showed that the binding affinity was weakest for the fullerene and strongest for the graphene due to reduced efficiency of π-stacking interactions between the aromatic side chains of the peptide and the fullerene and CNT arising from the increased surface curvature (Todorova et al 2013).…”

Section: Morphologymentioning

confidence: 99%

Modeling and simulation of protein–surface interactions: achievements and challenges

Ozboyaci

Kokh

Corni

et al. 2016

Quart. Rev. Biophys.

197

199

View full text Add to dashboard Cite

Abstract. Understanding protein-inorganic surface interactions is central to the rational design of new tools in biomaterial sciences, nanobiotechnology and nanomedicine. Although a significant amount of experimental research on protein adsorption onto solid substrates has been reported, many aspects of the recognition and interaction mechanisms of biomolecules and inorganic surfaces are still unclear. Theoretical modeling and simulations provide complementary approaches for experimental studies, and they have been applied for exploring protein-surface binding mechanisms, the determinants of binding specificity towards different surfaces, as well as the thermodynamics and kinetics of adsorption. Although the general computational approaches employed to study the dynamics of proteins and materials are similar, the models and force-fields (FFs) used for describing the physical properties and interactions of material surfaces and biological molecules differ. In particular, FF and water models designed for use in biomolecular simulations are often not directly transferable to surface simulations and vice versa. The adsorption events span a wide range of time-and length-scales that vary from nanoseconds to days, and from nanometers to micrometers, respectively, rendering the use of multi-scale approaches unavoidable. Further, changes in the atomic structure of material surfaces that can lead to surface reconstruction, and in the structure of proteins that can result in complete denaturation of the adsorbed molecules, can create many intermediate structural and energetic states that complicate sampling. In this review, we address the challenges posed to theoretical and computational methods in achieving accurate descriptions of the physical, chemical and mechanical properties of protein-surface systems. In this context, we discuss the applicability of different modeling and simulation techniques ranging from quantum mechanics through all-atom molecular mechanics to coarse-grained approaches. We examine uses of different sampling methods, as well as free energy calculations. Furthermore, we review computational studies of protein-surface interactions and discuss the successes and limitations of current approaches.

show abstract

Section: Morphologymentioning

confidence: 99%

Modeling and simulation of protein–surface interactions: achievements and challenges

Ozboyaci

Kokh

Corni

et al. 2016

Quart. Rev. Biophys.

197

199

View full text Add to dashboard Cite

show abstract

“…A part of the free imidazole groups of the mediator polymer would adsorb on CNT surfaces via π -π interaction. [ 28 ] The adsorption density of PVI-[Os(bpy) 2 Cl] calculated using the effective inner surface area of the CNTF fi lms (8.2 cm 2 for 20 μ m thick fi lm) [ 21 ] was (1.6 ± 0.1) × 10 − 10 mol cm…”

Section: Adsorption Of Pvi-[os(bpy) 2 Cl] Inside Cntf Filmsmentioning

confidence: 99%

“…The anionic GOD molecules could be stably entrapped by electrostatic interaction with cationic Os-complex of the mediator polymer that is anchored on the CNT surface via π -π interaction. [ 28 ] The electron-transfer turnover rate for the 20 μ m thick fi lm was calculated from the current value at 25 ° C (0.29 mA), the Faraday constant (96 500 C mol − 1 ), the molecular weight of GOD (186 000 g mol − 1 ), and the content of GOD molecules in …”

Section: Application As a Flexible Anode Of Biofuel Cellsmentioning

confidence: 99%

Molecularly Ordered Bioelectrocatalytic Composite Inside a Film of Aligned Carbon Nanotubes

Yoshino

Miyake

Yamada

et al. 2012

Advanced Energy Materials

View full text Add to dashboard Cite

Molecularly ordered composites of polyvinylimidazole‐[Os(bipyridine)2Cl] (PVI‐[Os(bpy)2Cl]) and glucose oxidase (GOD) are assembled inside a film of aligned carbon nanotubes. The structure of the prepared GOD/PVI‐[Os(bpy)2Cl]/CNT composite film is entirely uniform and stable; more than 90% bioelectrocatalytic activity could be maintained even after storage for 6 d. Owing to the ideal positional relationship achieved between enzyme, mediator, and electrode, the prepared film shows a high bioelectrocatalytic activity for glucose oxidation (ca. 15 mA cm−2 at 25 °C) with an extremely high electron‐transfer turnover rate (ca. 650 s−1) comparable to the value for GOD solutions, indicating almost every enzyme molecule entrapped within the ensemble (ca. 3 × 1012 enzymes in a 1 mm × 1 mm film) can work to the fullest extent. This free‐standing, flexible composite film can be used by winding on a needle device; as an example, a self‐powered sugar monitor is demonstrated.

show abstract

“…Thus, the addition of carbon nanotubes has no significant influence on the concentration of either the reactant or the organocatalyst and hence the observed effect on the HPESW reaction is likely to be related to the altered properties of the organocatalyst by transient non-covalent interactions with carbon nanotubes. Carbon nanotubes and fullerenes are known to form relatively strong non-covalent interactions with a wide range of amines 22 and amino acids, [23][24][25][26][27] including proline. [28][29][30][31] Whilst the nature of interactions between proline and carbon nanostructures is still not definitively understood, the exact mechanism is likely to reflect a number of cooperative forces, including ionic interactions, 32 N-H … π hydrogen bonding interactions 33 and electron transfer interactions.…”

Section: Introductionmentioning

confidence: 99%

The effects of interactions between proline and carbon nanostructures on organocatalysis in the Hajos–Parrish–Eder–Sauer–Wiechert reaction

Rance

Khlobystov

2014

Nanoscale

View full text Add to dashboard Cite

A note on versions:The version presented here may differ from the published version or from the version of record. If you wish to cite this item you are advised to consult the publisher's version. Please see the repository url above for details on accessing the published version and note that access may require a subscription. The non-covalent interactions of S-(-)-proline with the surfaces of carbon nanostructures (fullerene, nanotubes and graphite) change the nucleophilic-electrophilic and acid-base properties of the amino acid, thus tuning its activity and selectivity in the organocatalytic HajosParrish-Eder-Sauer-Wiechert (HPESW) reaction. Whilst our spectroscopy and microscopy measurements show no permanent covalent bonding between S-(-)-proline and carbon nanostructures, a systematic investigation of the catalytic activity and selectivity of the organocatalyst in the HPESW reaction demonstrates a clear correlation between the pyramidalisation angle of carbon nanostructures and the catalytic properties of S-(-)-proline. Carbon nanostructures with larger pyramidalisation angles have a stronger interaction wit h the nitrogen atom lone pair of electrons of the organocatalyst, thereby simultaneously decreasing the nucleophilicity and increasing the acidity of the organocatalyst. These translate into lower conversion rates but higher selectivities towards the dehydrated product of Aldol addition.

show abstract

Amino acid adsorption on single-walled carbon nanotubes

Cited by 69 publications

References 13 publications

Modeling and simulation of protein–surface interactions: achievements and challenges

Modeling and simulation of protein–surface interactions: achievements and challenges

Molecularly Ordered Bioelectrocatalytic Composite Inside a Film of Aligned Carbon Nanotubes

The effects of interactions between proline and carbon nanostructures on organocatalysis in the Hajos–Parrish–Eder–Sauer–Wiechert reaction

Contact Info

Product

Resources

About