Protein Immobilization onto Cationic Spherical Polyelectrolyte Brushes Studied by Small Angle X-ray Scattering

Li, Li; Henzler, Katja; Lü, Yan; Wang, Junyou; Han, Haoya; Tian, Yanhua; Wang, Yunwei; Zhou, Zhi; Lötze, Gudrun; Narayanan, Theyencheri; Ballauff, Matthias; Guo, Xuhong

doi:10.1021/acs.biomac.7b00164

Cited by 39 publications

(68 citation statements)

References 58 publications

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“…Additionally, it is worth noting that in order to eliminate the possible influence of interference of pure fluorescein pH response characteristics on experimental results, different fluorescence calibration curves under different experimental conditions were obtained and used. Compared with the commonly used quantitative method, that is, UV–Vis spectroscopy, fluorescence spectroscopy is more intuitive and convenient as no further ultrafiltration or centrifugation is required.…”

Section: Methodsmentioning

confidence: 99%

“…The scattering intensity of an SPB particle which has already bonded with a given amount of proteins can be divided into three independent parts:

I_{0} ((), q) = I_{cs} ((), q) + I_{ps} ((), q) + I_{fluct} ((), q)

…”

Section: Methodsmentioning

confidence: 99%

“…This part dominates the scattering intensity at small scattering angles. For a spherical symmetric particle, this term is equal to the square of the scattering amplitude B ( q ), which could be described as shown below:

B ((), q) = 4 italicπb \int_{0}^{R} ([], ρ^{e} ((), r) - ρ_{m}^{e}) r^{2} \frac{sin italicqr}{qr} italicdr

where b is the Thomson scattering length and equal to 0.282 × 10 −14 m. R is the radius of the spherical particle, and (

ρ^{e} ((), r) - ρ_{m}^{e}

), that is, Δρ e ( r ), denotes the difference between the radial electron density of the particle ρ e ( r ) and the electron density of solvent

ρ_{m}^{e}

. Hence, it is obvious that the higher the contrast of electron density between particle and solvent is, the stronger the scattering signal will be.…”

Section: Methodsmentioning

confidence: 99%

“…Small angle X‐ray scattering (SAXS) is an important method which is often used to analyze the distribution of proteins within polyelectrolyte brushes and the interaction between them. When SAXS is applied to protein‐immobilized SPB, through the analysis of the change of the excess electron density (Δ ρ e ), the location and the migration of the protein nanoparticles within the shell become “visible.”…”

Section: Introductionmentioning

confidence: 99%

“…To our best knowledge, this is the first combination of these two effective means to study the adsorption and desorption of proteins by SPB. And to eliminate the interference caused by the change of polyelectrolyte structure and gain more detailed and reliable insight into the interaction mechanism between protein and polyelectrolyte chains of SPB, the quenched SPB (Q‐SPB) were selected where the grafted polymer chains are strong polyelectrolytes and nearly don't respond to external environment.…”

Section: Introductionmentioning

confidence: 99%

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Controllable immobilization of proteins in quenched spherical polyelectrolyte brushes as observed by fluorescence spectroscopy and small angle X‐ray scattering

Zhao

et al. 2018

J Polym Sci B Polym Phys

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The immobilization of lysozymes (pI = 11) onto anionic spherical polyelectrolyte brushes (SPB) which consist of a solid polystyrene core and a densely grafted poly(styrene sulfonate) (PSS) shell was systematically studied by fluorescence spectroscopy and small angle X‐ray scattering. Results show that the capture of lysozyme by PSS brush is a dynamic process, which involves a quick agglomeration stage and a slow rearrangement one. And lysozyme inclines to immobilize in the inner layer of the brush, and saturation of lysozyme adsorption onto the SPB is gradually reached as the protein concentration increases, proceeding from the inside to the outside of the brush layers. As increasing the pH and ionic strength, the lysozyme previously adsorbed will be partially released and migrate from the inner to the outer layer of SPB. Last competitive adsorption tests between lysozyme and BSA or β‐glucosidase were performed, indicating that besides electrostatic interaction counterion release force also plays an important role in protein adsorption. SPB was proved to be ideal candidate for controllable immobilization of protein, which can be extended into various applications, such as drug delivery and protein separation. © 2018 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2018, 56, 1577–1588

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Section: Methodsmentioning

confidence: 99%

“…The scattering intensity of an SPB particle which has already bonded with a given amount of proteins can be divided into three independent parts:

I_{0} ((), q) = I_{cs} ((), q) + I_{ps} ((), q) + I_{fluct} ((), q)

…”

Section: Methodsmentioning

confidence: 99%

B ((), q) = 4 italicπb \int_{0}^{R} ([], ρ^{e} ((), r) - ρ_{m}^{e}) r^{2} \frac{sin italicqr}{qr} italicdr

where b is the Thomson scattering length and equal to 0.282 × 10 −14 m. R is the radius of the spherical particle, and (

ρ^{e} ((), r) - ρ_{m}^{e}

), that is, Δρ e ( r ), denotes the difference between the radial electron density of the particle ρ e ( r ) and the electron density of solvent

ρ_{m}^{e}

. Hence, it is obvious that the higher the contrast of electron density between particle and solvent is, the stronger the scattering signal will be.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Controllable immobilization of proteins in quenched spherical polyelectrolyte brushes as observed by fluorescence spectroscopy and small angle X‐ray scattering

Zhao

et al. 2018

J Polym Sci B Polym Phys

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Structure and Functionality of Polyelectrolyte Brushes: A Surface Force Perspective

Billing

Ruths

et al. 2018

Chemistry An Asian Journal

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The unique functionality of polyelectrolyte brushes depends on several types of specific interactions, including solvent structure effects, hydrophobic forces, electrostatic interactions, and specific ion interactions. Subtle variations in the solution environment can lead to conformational and surface structural changes of the polyelectrolyte brushes, which are mainly discussed from a surface-interaction perspective in this Focus Review. A brief overview is given of recent theoretical and experimental progress in the structure of polyelectrolyte brushes in various environments. Two important techniques for surface-force measurements are described, the surface forces apparatus (SFA) and atomic force microscopy (AFM), and some recent results on polyelectrolyte brushes are shown. Lastly, this Focus Review highlights the use of these surface-grafted polyelectrolyte brushes in the creation of functional surfaces for various applications, including nonfouling surfaces, boundary lubricants, and stimuli-responsive surfaces.

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Selective uptake of different proteins by annealed and quenched cationic spherical polyelectrolyte brushes

Dai

et al. 2020

Journal of Polymer Science

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Protein Immobilization onto Cationic Spherical Polyelectrolyte Brushes Studied by Small Angle X-ray Scattering

Cited by 39 publications

References 58 publications

Controllable immobilization of proteins in quenched spherical polyelectrolyte brushes as observed by fluorescence spectroscopy and small angle X‐ray scattering

Controllable immobilization of proteins in quenched spherical polyelectrolyte brushes as observed by fluorescence spectroscopy and small angle X‐ray scattering

Structure and Functionality of Polyelectrolyte Brushes: A Surface Force Perspective

Selective uptake of different proteins by annealed and quenched cationic spherical polyelectrolyte brushes

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