Dataset Information

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

ABSTRACT: 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.

SUBMITTER: Walkowiak J

PROVIDER: S-EPMC7795234 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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

Walkowiak Jacek J Gradzielski Michael M Zauscher Stefan S Ballauff Matthias M

Polymers 20201230 1

We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of <i>tert</i>-butyl acrylate (<i>t</i>BA) 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 i ...[more]

PMID: 33396873

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Project description:BackgroundThe presence of lignin normally affects enzymatic saccharification of lignocellulose detrimentally. However, positive effects of lignin on enzymatic hydrolysis have been recently reported. Enzyme-lignin interactions could be the key to reveal the underlying mechanism of their discrepant behaviors. In this study, to elucidate the positive effects of extractable lignin (EL) on enzymatic hydrolysis of ethanol organosolv-pretreated wood sawdust, two lignin fractions, EL and milled wood lignin (MWL), were isolated sequentially from pretreated substrates. Quartz crystal microbalance with dissipation (QCM-D) was then used to investigate the lignin aggregation effects on enzyme adsorption.ResultsWe found that both EL and MWL had a narrow molecular weight distribution. However, MWL had an obviously higher molecular weight than EL. This indicated that EL and MWL likely represent two distinct lignin fractions from ethanol organosolv-pretreated substrates. HSQC NMR analysis revealed that less β-O-4, β-β, and β-5 linkages and a higher S/G ratio was present in EL, as compared to MWL. QCM-D analysis showed that the enzyme adsorption on lignin was highly relevant to these lignin structural characteristics. An obviously lower maximum enzyme adsorption capacity was observed on EL films (152.63-168.09 ng/cm2) compared to MWL films (196.71-224.73 ng/cm2). Furthermore, enzyme desorption on lignin films was determined. A significantly lower irreversible enzyme adsorption was observed on EL (75.40 ng/cm2) compared to MWL (137.35 ng/cm2). More importantly, two reconstructed lignin films were designed to investigate lignin assembly on enzyme adsorption. The results indicated that the presence of EL reduced irreversible enzyme adsorption on the reconstructed lignin films by 39.2-45.0%.ConclusionsLignin structure determined the interaction between enzyme and lignins. A positive correlation was observed between molecular weight, the content of β-5 linkages, and enzyme adsorption on lignin. EL, which was more depolymerized and less condensed, had the lower enzyme adsorption of the two preparations tested. Additionally, the presence of EL reduced enzyme adsorption on reconstructed lignin films, perhaps through a mechanism involving the blocking of non-productive enzyme binding sites on the MWL. This could be the mechanism for the positive effects of EL on enzymatic hydrolysis.

Dataset Information

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

Publications

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

Similar Datasets

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