Insights on structural variations of protein adsorption layers on hydrophobic fluorohydrocarbon polymers gained by spectroscopic ellipsometry (part I)

Werner, Carsten; Eichhorn, K.‐J.; Grundke, Karina; Simon, Frank; Grählert, Wulf; Jacobasch, H.‐J.

doi:10.1016/s0927-7757(99)00007-2

Cited by 98 publications

(106 citation statements)

References 32 publications

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“…The two Stokes parameters Δ (phase shift) and Ψ (amplitude ratio) were calculated using an optical 4 phases model (Si/SiO 2 /polymer/ambient) [16]. The optical constants of Si and SiO 2 were taken from the literature [17,18]. The best fit results (without roughness correction) gave the effective refractive indices and thickness values for the overall polymer layer system on the wafer surface.…”

Section: Methodsmentioning

confidence: 99%

Sulfated cellulose thin films with antithrombin affinity

Grombe¹,

Gouzy²,

Freudenberg³

et al. 2009

Express Polym. Lett.

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Cellulose thin films were chemically modified by in situ sulfation to produce surfaces with anticoagulant characteristics. Two celluloses differing in their degree of polymerization (DP): CEL I (DP 215–240) and CEL II (DP 1300–1400) were tethered to maleic anhydride copolymer (MA) layers and subsequently exposed to SO3•NMe3 solutions at elevated temperature. The impact of the resulting sulfation on the physicochemical properties of the cellulose films was investigated with respect to film thickness, atomic composition, wettability and roughness. The sulfation was optimized to gain a maximal surface concentration of sulfate groups. The scavenging of antithrombin (AT) by the surfaces was determined to conclude on their potential anticoagulant properties

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Section: Methodsmentioning

confidence: 99%

Sulfated cellulose thin films with antithrombin affinity

Grombe¹,

Gouzy²,

Freudenberg³

et al. 2009

Express Polym. Lett.

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“…[44] The magnitude of the frequency shifts at the third, fifth, and seventh harmonic frequencies is shown as a function of composition in Figure 6b. While many studies employ a rinsing step to remove reversibly bound protein, [45][46][47] no rinsing was used in the current work. Thus, these data represent the total protein adsoprtion (reversible and irreversible) immediately after the introduction of protein to the copolymer surfaces.…”

Section: Protein Adsorption Experimentsmentioning

confidence: 99%

Random Copolymer Films with Molecular‐Scale Compositional Heterogeneities that Interfere with Protein Adsorption

Baxamusa

Gleason

2009

Adv Funct Materials

120

172

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Smooth surfaces with compositional heterogeneities at a molecular‐length scale are presented with the goal of disrupting surface–protein interactions. These surfaces are synthesized by utilizing photoinitiated chemical vapor deposition (piCVD) to deposit thin films of random copolymers consisting of highly hydrophilic and highly hydrophobic comonomers. Swellability, wettability, and surface roughness could be systematically controlled by tuning the copolymer composition. The surface composition was dynamic, and the surface reconstructed based on the hydration state of the film. Proteins adsorbed to the copolymer films less readily than to either of the respective homopolymers, indicating a synergistic effect resulting from the random copolymer presenting molecular‐scale compositional heterogeneity. These results provide direct evidence that protein adsorption can be disrupted by such surfaces and a simple analytical model suggests that the heterogeneities occur over areas encompassing 4–5 repeat units of the polymer. The synthetic method used to create these films can be used to coat arbitrary geometries, enabling practical utility in a number of applications.

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“…FIB's refractive index n(ω = 0 eV) increases with time at pH 7.4, from 1.326 to 1.375, which means that the initially the FIB layer formed on a-C:H film adsorbs at higher energies, which decrease as the volume fraction of adsorbed FIB increases with time. The value of the refractive index is in good agreement with [30], although a different simpler model is used. However, at pI, n(ω = 0 eV) remains almost constant (1.340 to 1.347), although FIB's adsorbed state increases with time (Fig.…”

mentioning

confidence: 54%

“…The high value of the thickness (~80 nm) is also attributed to the high concentration of the protein solution (1 mg/ml). That is, the concentration of the protein solution affects the thickness of the adsorbed protein [30]. In Fig.…”

mentioning

confidence: 99%

Real‐time spectroscopic ellipsometry for protein adsorption study and pH effect

Lousinian

Logothetidis

2008

Phys. Status Solidi (c)

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Carbon based thin films, such as amorphous carbon (a‐C) and amorphous hydrogenated diamond‐like carbon (a‐C:H) are considered as excellent candidates for biomedical applications. Protein adsorption is an important aspect for the improvement of many applications, such as medical implants, biosensor design, etc. The density, orientation, and conformation of surface‐bound proteins are believed to be key factors in controlling subsequent cellular adhesion. Aim of this work is the study of the pH effect on fibrinogen adsorption on a haemocompatible a‐C:H thin film developed by rf reactive magnetron sputtering. For this purpose, Vis–UV Spectroscopic Ellipsometry (SE) has been used. It is a non destructive, surface sensitive technique, with the capability of performing real‐time measurements in air as well as in liquid environment, with great potential in biomedical studies. An appropriate ellipsometric model has been developed, in order to describe accurately the protein adsorption mechanisms in real‐time. SE results reveal the differences in the rate of fibrinogen thickness increase and transition rate of fibrinogen from liquid to adsorbed state. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

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Insights on structural variations of protein adsorption layers on hydrophobic fluorohydrocarbon polymers gained by spectroscopic ellipsometry (part I)

Cited by 98 publications

References 32 publications

Sulfated cellulose thin films with antithrombin affinity

Sulfated cellulose thin films with antithrombin affinity

Random Copolymer Films with Molecular‐Scale Compositional Heterogeneities that Interfere with Protein Adsorption

Real‐time spectroscopic ellipsometry for protein adsorption study and pH effect

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