Temperature-Driven Adsorption and Desorption of Proteins at Solid–Liquid Interfaces

Kiesel, Irena; Paulus, Michael; Nase, Julia; Tiemeyer, Sebastian; Sternemann, Christian; Rüster, Karin; Wirkert, Florian J.; Mende, Kolja; Büning, Thomas; Tolan, Metin

doi:10.1021/la404884a

Cited by 28 publications

(35 citation statements)

References 44 publications

(60 reference statements)

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“…BSA and fibrinogen adsorption on the PET substrate at 37 °C was weaker than that at room temperature. This evidence supports our results in Table 2 and Figure 4 , whereas several studies have indicated contrary results, i.e., that heating enhances protein adsorption on inorganic substrates, including silica and silicon [ 40 , 41 ]. The contradictory effect of temperature on protein adsorption is probably due to the differences in the surface chemistry of plastics and silicon oxide, which has polar groups.…”

Section: Discussionsupporting

confidence: 92%

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Effect of Temperature Changes on Serum Protein Adsorption on Thermoresponsive Cell-Culture Surfaces Monitored by A Quartz Crystal Microbalance with Dissipation

Kobayashi

Arisaka

Yui

et al. 2018

IJMS

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Thermoresponsive cell-culture polystyrene (PS) surfaces that are grafted with poly(N-isopropylacrylamide) (PIPAAm) facilitate the cultivation of cells at 37 °C and the detachment of cultured cells as a sheet with an underlying extracellular matrix (ECM) by reducing the temperature. However, the ECM and cell detachment mechanisms are still unclear because the detachment of cells from thermoresponsive surfaces is governed by complex interactions among the cells/ECM/surface. To explore the dynamic behavior of serum protein adsorption/desorption, thermoresponsive surfaces that correspond to thermoresponsive tissue-culture PS dishes were formed on sensor chips for quartz crystal microbalance with dissipation (QCM-D) measurements. X-ray photoelectron spectroscopy (XPS) measurements and temperature-dependent frequency and dissipation shifts, Δf and ΔD, using QCM-D revealed that the thermoresponsive polymers were successfully grafted onto oxidized, thin PS films on the surfaces of the sensor chips. Increased amounts of adsorbed bovine serum albumin (BSA) and fibronectin (FN) were observed on the thermoresponsive polymer-grafted surfaces at 37 °C when compared with those at 20 °C because of enhanced hydrophobic interactions with the hydrophobic, thermoresponsive surface. While the calculated masses of adsorbed BSA and FN using QCM-D were 3–5 times more than those that were obtained from radiolabeling, the values were utilized for relative comparisons among the same substrate. More importantly, the thermoresponsive, dynamic behavior of serum protein adsorption/desorption was monitored using the QCM-D technique. Observations of this dynamic behavior revealed that the BSA and FN that were adsorbed at 37 °C remained on both surfaces after decreasing the temperature to 20 °C.

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Section: Discussionsupporting

confidence: 92%

“…The degree of adsorption on these surfaces depended on the molecular weight of the proteins. The molecular weights of the proteins that were used in this study are as follows: BSA, 66,300; FN, 440,000 g/mol [ 41 ]. Therefore, the larger FN could be inhibited by steric hindrance from the hydrated and swollen thermoresponsive polymer chains.…”

Section: Discussionmentioning

confidence: 99%

Effect of Temperature Changes on Serum Protein Adsorption on Thermoresponsive Cell-Culture Surfaces Monitored by A Quartz Crystal Microbalance with Dissipation

Kobayashi

Arisaka

Yui

et al. 2018

IJMS

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“…The effect of temperature on the amount of adsorbed proteins on silicon wafers was studied for albumin and fibronectin. The adsorbed amount of these proteins remains constant in the range of 20 °C to 40 °C showing no significant desorption [29].…”

Section: Methodsmentioning

confidence: 96%

Serum protein layers on parylene-C and silicon oxide: Effect on cell adhesion

Delivopoulos

Ouberaï

Coffey

et al. 2015

Colloids and Surfaces B: Biointerfaces

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“…The X-ray reflectivity measurements were performed at the Bl9 beamline at the synchrotron light source DELTA in Dortmund, Germany [31][32][33][34]. We used hard X-rays with a photon energy of 27 keV (0.459 Å) to penetrate the liquid area without loss.…”

Section: In-situ X-ray Reflectivity (Xrr) Experimentsmentioning

confidence: 99%

Porous Ultra-Thin Films from Photocleavable Block Copolymers: In-Situ Degradation Kinetics Study of Pore Material

et al. 2020

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On the basis of the major application for block copolymers to use them as separation membranes, lithographic mask, and as templates, the preparation of highly oriented nanoporous thin films requires the selective removal of the minor phase from the pores. In the scope of this study, thin film of polystyrene-block-poly(ethylene oxide) block copolymer with a photocleavable junction groups based on ortho-nitrobenzylester (ONB) (PS-hν-PEO) was papered via the spin coating technique followed by solvent annealing to obtain highly-ordered cylindrical domains. The polymer blocks are cleaved by means of a mild UV exposure and then the pore material is washed out of the polymer film by ultra-pure water resulting in arrays of nanoporous thin films to remove one block. The removal of the PEO materials from the pores was proven using the grazing-incidence small-angle X-ray scattering (GISAXS) technique. The treatment of the polymer film during the washing process was observed in real time after two different UV exposure time (1 and 4 h) in order to draw conclusions regarding the dynamics of the removal process. In-situ X-ray reflectivity measurements provide statistically significant information about the change in the layer thickness as well as the roughness and electron density of the polymer film during pore formation. 4 H UV exposure was found to be more efficient for PEO cleavage. By in-situ SFM measurements, the structure of the ultra-thin block copolymer films was also analysed and, thus, the kinetics of the washing process was elaborated. The results from both measurements confirmed that the washing procedure induces irreversible change in morphology to the surface of the thin film.

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Temperature-Driven Adsorption and Desorption of Proteins at Solid–Liquid Interfaces

Cited by 28 publications

References 44 publications

Effect of Temperature Changes on Serum Protein Adsorption on Thermoresponsive Cell-Culture Surfaces Monitored by A Quartz Crystal Microbalance with Dissipation

Effect of Temperature Changes on Serum Protein Adsorption on Thermoresponsive Cell-Culture Surfaces Monitored by A Quartz Crystal Microbalance with Dissipation

Serum protein layers on parylene-C and silicon oxide: Effect on cell adhesion

Porous Ultra-Thin Films from Photocleavable Block Copolymers: In-Situ Degradation Kinetics Study of Pore Material

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