1998
DOI: 10.1016/s0142-9612(97)00223-8
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FTIR/ATR for protein adsorption to biomaterial surfaces

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Cited by 386 publications
(298 citation statements)
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“…The recorded amide II band intensities were below 1 mAU (Fig 1A). A very approximate comparison with a published study of amide II intensity of known concentration of standard proteins [37] suggests that such intensities are measured for maximum protein concentration of 0.05 g/cm 2 , i.e. in our system 0.0145 g of total immobilised protein.…”
Section: Hydrogen Evolution From the Electrodesmentioning
confidence: 55%
See 1 more Smart Citation
“…The recorded amide II band intensities were below 1 mAU (Fig 1A). A very approximate comparison with a published study of amide II intensity of known concentration of standard proteins [37] suggests that such intensities are measured for maximum protein concentration of 0.05 g/cm 2 , i.e. in our system 0.0145 g of total immobilised protein.…”
Section: Hydrogen Evolution From the Electrodesmentioning
confidence: 55%
“…Since cyclic voltammograms of hydrogenases always display catalytic currents, due to the presence of protons as substrate, the quantitation of the adsorbed protein in electroactive form is very difficult. The estimate amount of immobilised protein on surfaces by ATR-FTIR has been proposed in some systems on the basis of the recorded intensity of the amide I, II and III signals [37,38] but the quantitation suffers from several uncertainties due to the thickness of the system during cell assembly. In this case the measurements were performed on the protein adsorbed on the TiO2 electrode layered on the FTO 5 glass, a thick and fragile support, and the protein-TiO2 surface system was then placed in contact with the Germanium crystal and tightened.…”
Section: Hydrogen Evolution From the Electrodesmentioning
confidence: 99%
“…However, labeling may change the conformation stability of proteins, and affect their adsorption behavior or even promote aggregation in proteins [87,95,96]. To avoid the adverse effects of labeling, other "label-free" tools have been employed such as size exclusion chromatography [87,95,96], electrophoresis [128], ellipsometry [132,133], spectroscopy [134], surface plasmon resonance [101], quartz crystal microbalance [135], tensiometry [132], reflectrometry [136], shear rheology [125], surface force apparatus [137] and imaging techniques [138]. However, there are only a few reports where these tools have been employed on oligomers (monomers, dimers etc) of the same protein [87][88][89].…”
Section: Oligomeric Protein Adsorption-desorption To Es Silica Capillmentioning
confidence: 99%
“…The instrument has an 134 upper limit of 10 6 particles/cm 3 (in the aerosol phase), but any highly concentrated solution can always be diluted to reduce the concentration to the linear region of the instrument. Thus, the upper range can be defined by the highest particle titer in a test particle.…”
Section: Rangementioning
confidence: 99%
“…[4][5][6] In the ATR technique, the IR beam is totally reflected inside a waveguide. At each reflection an evanescent field is created at the surface of the waveguide.…”
mentioning
confidence: 99%