Increasing Protein Stability through Control of the Nanoscale Environment

Asuri, Prashanth; Karajanagi, Sandeep S.; Yang, Hoichang; Yim, Tae-Jin; Kane, Ravi S.; Dordick, Jonathan S.

doi:10.1021/la0528450

Cited by 186 publications

(176 citation statements)

References 19 publications

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“…The different effects of CNTs and GO on the enzymes activities and structures could be related to specific interactions of enzymes with these nanomaterials (Kim et al, 2008), as indicated by XRD results in Section 3.2. The positive effect on the lipases' catalytic behavior by CNTs could be also related by the increased curvature of CNTs compared to graphene oxide in a similar manner as described by Asuri et al for protein immobilization on single-walled CNTs (Asuri et al, 2006b). Namely, the increased curvature of CNTs could probably contribute to a reduction of detrimental interactions between immobilized protein molecules given that these molecules are further apart in this case; this in turn leads to increased enzyme stability on CNTs compared to that on flat graphene oxide.…”

Section: Structural Studiesmentioning

confidence: 67%

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

Pavlidis

Vorhaben

Tsoufis

et al. 2012

Bioresource Technology

140

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Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials Pavlidis, Ioannis V.; Vorhaben, Torge; Tsoufis, Theodoros; Rudolf, Petra; Bornscheuer, Uwe T.; Gournis, Dimitrios; Stamatis, Haralambos Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. a b s t r a c tIn this study we report the use of functionalized carbon-based nanomaterials, such as amine-functionalized graphene oxide (GO) and multi-walled carbon nanotubes (CNTs), as effective immobilization supports for various lipases and esterases of industrial interest. Structural and biochemical characterization have revealed that the curvature of the nanomaterial affect the immobilization yield, the catalytic behavior and the secondary structure of enzymes. Infrared spectroscopy study indicates that the catalytic behavior of the immobilized enzymes is correlated with their a-helical content. Hydrolases exhibit higher esterification activity (up to 20-fold) when immobilized on CNTs compared to GO. The covalently immobilized enzymes exhibited comparable or even higher activity compared to the physically adsorbed ones, while they presented higher operational stability. The enhanced catalytic behavior observed for most of the hydrolases covalently immobilized on amine-functionalized CNTs indicate that these functionalized nanomaterials are suitable for the development of efficient nanobiocatalytic systems.

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Section: Structural Studiesmentioning

confidence: 67%

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

Pavlidis

Vorhaben

Tsoufis

et al. 2012

Bioresource Technology

140

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“…Changes in secondary structure from a-helix to b-sheet were detected in a model peptide covalently attached to thiolated Au NPs [43]. Other surfaces with nanoscale curvature, such as liposomes [44] and single-walled carbon nanotubes [45,46], have been investigated for their effect on the catalytic activity of enzymes. These measurements suggested that proteins could be stabilized on surfaces with nanoscale curvature more readily than on flat surfaces by suppressing unfavourable lateral protein-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins

Kurylowicz

Paulin

Mogyoros

et al. 2014

J. R. Soc. Interface.

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ReviewCite this article: Kurylowicz M, Paulin H, Mogyoros J, Giuliani M, Dutcher JR. 2014 The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins. J. R. Soc. The influence of surface topography on protein conformation and association is used routinely in biological cells to orchestrate and coordinate biomolecular events. In the laboratory, controlling the surface curvature at the nanoscale offers new possibilities for manipulating protein-protein interactions and protein function at surfaces. We have studied the effect of surface curvature on the association of two proteins, a-lactalbumin (a-LA) and b-lactoglobulin (b-LG), which perform their function at the oil-water interface in milk emulsions. To control the surface curvature at the nanoscale, we have used a combination of polystyrene (PS) nanoparticles (NPs) and ultrathin PS films to fabricate chemically pure, hydrophobic surfaces that are highly curved and are stable in aqueous buffer. We have used single-molecule force spectroscopy to measure the contour lengths L c for a-LA and b-LG adsorbed on highly curved PS surfaces (NP diameters of 27 and 50 nm, capped with a 10 nm thick PS film), and we have compared these values in situ with those measured for the same proteins adsorbed onto flat PS surfaces in the same samples. The L c distributions for b-LG adsorbed onto a flat PS surface contain monomer and dimer peaks at 60 and 120 nm, respectively, while a-LA contains a large monomer peak near 50 nm and a dimer peak at 100 nm, with a tail extending out to 200 nm, corresponding to higher order oligomers, e.g. trimers and tetramers. When b-LG or a-LA is adsorbed onto the most highly curved surfaces, both monomer peaks are shifted to much smaller values of L c . Furthermore, for b-LG, the dimer peak is strongly suppressed on the highly curved surface, whereas for a-LA the trimer and tetramer tail is suppressed with no significant change in the dimer peak. For both proteins, the number of higher order oligomers is significantly reduced as the curvature of the underlying surface is increased. These results suggest that the surface curvature provides a new method of manipulating protein-protein interactions and controlling the association of adsorbed proteins, with applications to the development of novel biosensors.

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“…But in a high TYR concentration, probably the compact structure and multilayered formation of adjacent enzyme molecules result in a lower response. 63 The interfacial properties and the morphology of modified electrodes are of essential importance to get enough responses. We measured Rct value of different TYR concentration (0.05 mg/mL, 0.1 mg/mL, 0.25 mg/mL, 0.5 mg/mL, 1.0 mg/mL) on the GA/pTN/GC.…”

Section: Optimization Of Tyr Concentration Upon the Peak Current Respmentioning

confidence: 99%

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

Wang

Zhang

et al. 2017

Electrochemistry

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A stepwise strategy of mediator-free amperometric biosensor for the detection of catechol was developed based on the covalent bonding of tyrosinase (TYR) onto thionine (TN)-electrodeposited glassy carbon (GC) surface via glutaraldehyde (GA). Prior to the TYR-immobilization, poly(thionine) was prepared on a GC electrode surface by an electrooxidative polymerization of thionine. The TYR/GA/pTN modified electrode was evaluated by SEM and EIS measurements. The terminal amino groups (-NH 2 ) which electrodeposited on the GC surface were cross-linked with protein lysine group (or cysteine group) by GA. The resulting TYR/GA/pTN-immobilized GCE was utilized as a working electrode unit of a catechol-detect biosensor. Catechol was used as model analyte for the evaluation of catecholase activity, and the signal based on the electro-reduction of the enzymatically produced o-quinone species were monitored at −0.05 V vs. Ag/AgCl. The resulting TYR/GA/pTN/GCE biosensor exhibited rapid and sensitive response to catechol (100% response time: ≈5 s, sensitivity: 5.04 µA/mM, detection limit: 6.0 µM. The TYR/GA/ pTN/GCE retained 71% of original activity for catechol oxidation after 1 month storage.

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Increasing Protein Stability through Control of the Nanoscale Environment

Cited by 186 publications

References 19 publications

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

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