Adsorption/desorption behavior of protein on nanosized hydroxyapatite coatings: A quartz crystal microbalance study

The adsorption of Bovine Serum Albumin (BSA) on gold and titanium surfaces in Hanks’ solution was monitored using the electrochemical quartz crystal microbalance (EQCM) technique. The changes in mass and open circuit potential at rest potential and mass and current at constant potentials were measured before and after the introduction of BSA.The mass of BSA adsorbed on titanium reached a steady value within one hour, while the albumin adsorbed on gold continued to increase. The amount of BSA adsorbed by titanium increased with concentration and stabilized at 0.8 mg/ml while that on gold did not stabilize. This indicates a monolayer of the protein on titanium and multi-layer on gold. The adsorption of BSA on gold and titanium was accelerated by the charge of potential.The time before stabilizing the adsorption‒desorption phenomena also increased with the BSA concentration.

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Adsorption–Desorption Control of Fibronectin in Real Time at the Liquid/Polymer Interface on a Quartz Crystal Microbalance by Thermoresponsivity

Biomacromolecules ◽

10.1021/acs.biomac.9b00121 ◽

2019 ◽

Vol 20 (4) ◽

pp. 1748-1755 ◽

Cited By ~ 7

Author(s):

Jiatu Li ◽

Taisei Kaku ◽

Yuki Tokura ◽

Ko Matsukawa ◽

Kenta Homma ◽

...

Keyword(s):

Real Time ◽

Quartz Crystal Microbalance ◽

Quartz Crystal ◽

Liquid Polymer ◽

Polymer Interface ◽

Adsorption Desorption

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Interaction of Proteins with a Planar Poly(acrylic acid) Brush: Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)

Polymers ◽

10.3390/polym13010122 ◽

2020 ◽

Vol 13 (1) ◽

pp. 122

Author(s):

Jacek Walkowiak ◽

Michael Gradzielski ◽

Stefan Zauscher ◽

Matthias Ballauff

Keyword(s):

Acrylic Acid ◽

Quartz Crystal Microbalance ◽

Quartz Crystal ◽

Water Contact ◽

Strong Adsorption ◽

Ft Ir ◽

Calorimetric Studies ◽

Adsorption Desorption ◽

Contact Angle Analysis ◽

Poly Acrylic Acid

We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of tert-butyl acrylate (tBA) and subsequent acid hydrolysis, on the flat gold surfaces of quartz-crystal microbalance (QCM) crystals. The PAA brushes were characterized by Fourier transform infrared (FT-IR) spectroscopy, ellipsometry and water contact angle analysis. The interaction of the PAA brushes with human serum albumin (HSA) was studied for a range of ionic strengths and pH conditions by quartz-crystal microbalance with dissipation monitoring (QCM-D). The quantitative analysis showed a strong adsorption of protein molecules onto the PAA brush. By increasing the ionic strength, we were able to release a fraction of the initially bound HSA molecules. This finding highlights the importance of counterions in the polyelectrolyte-mediated protein adsorption/desorption. A comparison with recent calorimetric studies related to the binding of HSA to polyelectrolytes allowed us to fully analyze the QCM data based on the results of the thermodynamic analysis of the binding process.

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