Optical properties of proteins and protein adsorption study

Lousinian, S.; Logothetidis, S.

doi:10.1016/j.mee.2006.10.082

Cited by 32 publications

(23 citation statements)

References 30 publications

(31 reference statements)

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“…Spectroscopic Ellipsometry Ellipsometry and UV-vis SE are often used to investigate adsorption dynamics at surfaces and thickness of thin and ultrathin biological films [22][23][24][25][26] and other complex molecular systems [7,8,[27][28][29][30][31].…”

Section: Methodsmentioning

confidence: 99%

Yeast Cytochrome c Monolayer on Flat and Nanostructured Gold Films Studied by UV–Vis Spectroscopic Ellipsometry

et al. 2011

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Spectroscopic ellipsometry (SE) has been used to investigate the adsorption of yeast cytochrome c (YCC) on gold films. YCC is a prototypical molecular system to evaluate the sensitivity and reliability of optical methods in probing conformational changes upon adsorption at surfaces. Measurements have been performed in situ in aqueous solutions at room temperature. We have applied to monolayer-thick YCC films the same scheme of analysis of SE spectra used in our recent works on thiolate self-assembled monolayers on gold, exploiting the so-called δ and δ difference spectra. A comparison between δ and δ spectra obtained from YCC adsorption on flat and cluster-assembled nanostructured gold films, obtained by supersonic cluster beam deposition is proposed. For both kinds of substrate δ and δ , difference spectra show well-defined features related to molecular optical absorptions typical of the so-called heme group, in particular the Soret band at about 410 nm. These features appear in the same position found for molecules in solution, suggesting that YCC native conformation is maintained upon adsorption also in the case of a substrate with typical roughness at the nanoscale.

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Section: Methodsmentioning

confidence: 99%

Yeast Cytochrome c Monolayer on Flat and Nanostructured Gold Films Studied by UV–Vis Spectroscopic Ellipsometry

et al. 2011

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“…These modifications provided control of the hydrodynamic conditions as well as the flux of protein to the titania surface. Although characterization of the flow cell was outside the scope of the present manuscript, the experimental setup is an alternative to the ones used by either Arwin [29, 43] or Logothetidis [44] and enables performing adsorption experiments under stagnation-point conditions.…”

Section: Methodsmentioning

confidence: 99%

Dynamic adsorption of albumin on nanostructured TiO 2 thin films

Wehmeyer

Synowicki

Bizios

et al. 2010

Materials Science and Engineering: C

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Spectroscopic ellipsometry was used to characterize the optical properties of thin (<5 nm) films of nanostructured titanium dioxide (TiO 2 ). These films were then used to investigate the dynamic adsorption of bovine serum albumin (BSA, a model protein), as a function of protein concentration, pH, and ionic strength. Experimental results were analyzed by an optical model and revealed that hydrophobic interactions were the main driving force behind the adsorption process, resulting in up to 3.5 mg/m 2 of albumin adsorbed to nanostructured TiO 2 . The measured thickness of the adsorbed BSA layer (less than 4 nm) supports the possibility that spreading of the protein molecules on the material surface occurred. Conformational changes of adsorbed proteins are important because they may subsequently lead to either accessibility or inaccessibility of bioactive sites which are ligands for cell interaction and function relevant to physiology and pathology.

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“…It measures the change of polarization of a light beam upon reflection off a sample and correlates it to the sample's thickness and refractive index, but beyond this basic principle, various ellipsometric techniques have been developed like the phase-modulated and the spectroscopic ellipsometry [56]. The later has an increased sensitivity for measurements on multilayered samples and, for this reason, has been extensively used in the study of protein adsorption on modified surfaces [57].…”

Section: Techniques To Study Protein Adsorptionmentioning

confidence: 99%