Factors that Affect Protein Adsorption on Nanostructured Titania Films. A Novel Spectroelectrochemical Application to Sensing

Topoglidis, Emmanuel; Campbell, Colin J.; Cass, and Anthony E. G.; Durrant, James R.

doi:10.1021/la010309b

Cited by 179 publications

(156 citation statements)

References 33 publications

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“…These proteins were selected as their different IEP (10.5 and 4.5 for Cyt-c and GFP, respectively [4]) allow a direct study of the importance of electrostatic interactions in controlling protein immobilization on the TiO 2 electrodes (pzc of ca. 5.5), as we have demonstrated previously [2,4]. At pH > 5.5, the TiO 2 electrode is therefore expected to exhibit a negative surface charge.…”

Section: Protein Adsorption Studiessupporting

confidence: 57%

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Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes

et al. 2005

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The immobilization of two acidic, low isoelectric point proteins, green fluorescence protein and ferredoxin (FRD) is investigated on nanocrystalline, mesoporous TiO 2 and SnO 2 electrodes. Modification of these electrodes with a cationic polypeptide (poly-l-lysine) or an aminosilane prior to protein immobilization is found to enhance protein binding at least ten fold, attributed to more favorable protein/electrode electrostatic interactions. Cyclic voltammetry studies of FRD-modified SnO 2 electrodes indicate reversible protein electrochemistry with a midpoint potential of À 0.59 V (vs. Ag/AgCl) and an interfacial electron transfer rate constant of 0.45 s À1 .

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Section: Protein Adsorption Studiessupporting

confidence: 57%

“…Employing a protein cross-sectional area of 415 2 , and using a SnO 2 film surface area of 300 cm 2 determined from BET analysis, these data yield surface coverages of 0.94 and 0.85 of a monolayer on the PLL-SnO 2 and AP-SnO 2 electrodes, respectively…”

mentioning

confidence: 99%

Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes

et al. 2005

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“…The oxidation process could be further accelerated by bubbling the solution with oxygen whilst applying þ 0.4 V. However, each complete cycle resulted in 5 -6% protein desorption, limiting the repeated use of a single film to 3 -4 separate binding titrations. The use of a thicker (8 instead of 4 mm) titania film, which exhibits double the amount of adsorbed Hb as reported previously [20] could overcome this limitation as the same film could be used twice the times, which would be adequate for this sensor. …”

mentioning

confidence: 89%

“…Spectroscopic measurements such as those shown in Figure 3 correspond to optical sensing of NO concentration and an optical aerobic biosensor can be developed [20].…”

Section: Electrochemical No Biosensormentioning

confidence: 99%

Nitric Oxide Biosensors Based on the Immobilization of Hemoglobin on Mesoporous Titania Electrodes

Topoglidis

Campbell

Cass³

et al. 2006

Electroanalysis

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A nanocrystalline TiO 2 film is an electrode material with large surface area which allows high levels of protein adsorption without loss of protein structure or activity. As an optically transparent semiconductor, titania can be used to carry out direct spectroelectrochemistry of proteins such as hemoglobin. We demonstrate that the high protein loading and the optical transparency and electrical conductivity of the Hb/TiO 2 films allow the optical and/or electrochemical sensing of nitric oxide. In particular we demonstrate the nitric oxide cycle of oxyhemoglobin immobilized on TiO 2 films and use it to electrochemically measure micromolar levels of nitric oxide.

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“…The surface fraction of all of the proteins studied was found to be concentration-dependent, with the presence of a second upper layer at higher concentrations. As for adsorption of FIII9-10 to the negatively charged SiO 2 surface [27], adsorption of FIII9 0 10 and FIII9 0 10-H2P to the negatively charged TiO 2 surface at approximately pH 6 [34] was likely to be driven by electrostatic interactions with the arginine cluster of FIII9 (Arg-1358, 1360, 1369, 1371, 1374, 1379-which can be readily visualized and compared against the relatively weak cationic face of FIII10 [27]). …”

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confidence: 99%

Interrogating protonated/deuterated fibronectin fragment layers adsorbed to titania by neutron reflectivity and their concomitant control over cell adhesion

McIntosh

Whitelaw

Rekas

et al. 2015

J. R. Soc. Interface.

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The fibronectin fragment, 9th-10th-type III domains (FIII9-10), mediates cell attachment and spreading and is commonly investigated as a bioadhesive interface for implant materials such as titania (TiO 2 ). How the extent of the cell attachment-spreading response is related to the nature of the adsorbed protein layer is largely unknown. Here, the layer thickness and surface fraction of two FIII9-10 mutants (both protonated and deuterated) adsorbed to TiO 2 were determined over concentrations used in cell adhesion assays. Unexpectedly, the isotopic forms had different adsorption behaviours. At solution concentrations of 10 mg l 21 , the surface fraction of the less conformationally stable mutant (FIII9 0 10) was 42% for the deuterated form and 19% for the protonated form (fitted to the same monolayer thickness). Similarly, the surface fraction of the more stable mutant (FIII9 0 10-H2P) was 34% and 18% for the deuterated and protonated forms, respectively. All proteins showed a transition from monolayer to bilayer between 30 and 100 mg l 21, with the protein longitudinal orientation moving away from the plane of the TiO 2 surface at high concentrations. Baby hamster kidney cells adherent to TiO 2 surfaces coated with the proteins (100 mg l 21) showed a strong spreading response, irrespective of protein conformational stability. After surface washing, FIII9 0 10 and FIII9 0 10-H2P bilayer surface fractions were 30/25% and 42/ 39% for the lower/upper layers, respectively, implying that the cell spreading response requires only a partial protein surface fraction. Thus, we can use neutron reflectivity to inform the coating process for generating bioadhesive TiO 2 surfaces.

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Factors that Affect Protein Adsorption on Nanostructured Titania Films. A Novel Spectroelectrochemical Application to Sensing

Cited by 179 publications

References 33 publications

Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes

Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes

Nitric Oxide Biosensors Based on the Immobilization of Hemoglobin on Mesoporous Titania Electrodes

Interrogating protonated/deuterated fibronectin fragment layers adsorbed to titania by neutron reflectivity and their concomitant control over cell adhesion

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