Structure of bovine serum albumin adsorbed on silica investigated by quartz crystal microbalance

Jachimska, Barbara; Tokarczyk, Karolina; Łapczyńska, Marta; Puciul-Malinowska, Agnieszka; Zapotoczny, Szczepan

doi:10.1016/j.colsurfa.2015.10.033

Cited by 89 publications

(110 citation statements)

References 28 publications

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“…The associated zeta potentials were calculated using Henry's equation, [3], and displayed in Figure 3. The zeta potential curve for Lysozyme in a solution with ionic strength I = 1 x 10 -2 M compares well with previously published results 33 .The isoelectric point of Lysozyme in this case is approximately 10.0, in agreement with previous results 26 . In the case of lysozyme AuNC nucleation dramatically changes the zeta potential.…”

Section: Resultssupporting

confidence: 92%

“…Before each measurement the sensor was cleaned using the same protocol each time. The Sauerbrey model was utilized in order to correlate changes to the frequency at which the quartz crystal resonated at to the mass of protein adsorbed to the sensor surface 26 . When adsorption occurs on the sensors' electrode surface the total mass increases, causing the resonant frequency (f) decrease.…”

Section: Methodsmentioning

confidence: 99%

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Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Russell

Jachimska

Komorek

et al. 2017

Phys. Chem. Chem. Phys.

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The study of gold nanoclusters (AuNCs) has seen much interest in recent history due to their unique fluorescence properties and environmentally friendly synthesis method using proteins as a growth scaffold. The differences in the physicochemical properties of lysozyme encapsulated AuNCs in comparison to natural lysozyme are characterised in order to determine the effects AuNCs have on natural protein behaviour. The hydrodynamic radius (dynamic light scattering), light absorbance (UV-Vis), electrophoretic mobility, relative density, dynamic viscosity, adsorption (quartz crystal microbalance) and circular dichroism (CD) characteristics of the molecules were studied. It was found that lysozyme forms small dimer/trimer aggregates upon the synthesis of AuNCs within the protein. The diameter of Ly-AuNCs was found to be 8.0 nm across a pH range of 2-11 indicating dimer formation, but larger aggregates with diameters >20 nm were formed between pH 3 and 6. The formation of larger aggregates limits the use of Ly-AuNCs as a fluorescent probe in this pH range. A large shift in the protein's isoelectric point was also observed, shifting from 11.0 to 4.0 upon AuNC synthesis. This resulted in major changes to the adsorption characteristics of lysozyme, observed using a QCM. A monolayer of 8 nm was seen for Ly-AuNCs at pH 4, offering further evidence that the proteins form small aggregates, unlike the natural monomer form of lysozyme. The adsorption of Ly-AuNCs was seen to decrease as pH was increased; this is in major contrast to the lysozyme adsorption behaviour. A decrease in the α-helix content was observed from 25% in natural lysozyme to 1% in Ly-AuNCs. This coincided with an increase in the β-sheet content after AuNC synthesis indicating that the natural structure of lysozyme was lost. The formation of protein dimers, the change in the protein surface charge from positive to negative, and secondary structure alteration caused by the AuNC synthesis must be considered before attempting to utilise Ly-AuNCs as in vivo probes.

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Section: Resultssupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Russell

Jachimska

Komorek

et al. 2017

Phys. Chem. Chem. Phys.

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“…This explains the fluctuation in corona thickness around 1–2 nm. These results are consistent with those of Jachimska et al, who showed that the maximum height of individual BSA adsorbed on a silica chip was 1.0 ± 0.2 nm. This suggests that BSA only formed a monomolecular layer on the GNP surface at low concentrations.…”

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confidence: 55%

Concurrent Detection of Protein Adsorption on Mixed Nanoparticles by Differential Centrifugal Sedimentation

Wang

Chen

et al. 2017

Part & Part Syst Charact

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In mixtures of nanoparticles of various sizes or compositions, monitoring protein partitioning on their surfaces provides important information about particle–protein interactions during competitive adsorption. Utilizing the size‐resolving capability of differential centrifugal sedimentation, the adsorption of bovine serum albumin on multisize gold nanoparticles with diameters ranging from 20 to 100 nm or gold, silver, and silica nanoparticles with similar diameter can be concurrently observed. This method can be used to gain insight into nanoparticle–protein interactions based on analyses of curvature and relative abundance.

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“…Upon adsorption on solid substrates, the dimensions of albumin are ranging from 9.2 Â 9.2 Â 3.0 nm (triangular shape) on surfaces with low adhesion, to 25.0 Â 2.1 Â 2.1 nm (elongated shape) on surfaces with larger adhesion. 13 In comparison, the hydrodynamic radius, R H , of BSA in solution is ranging from 3.3 to 4.3 nm. 14 The isoelectric point of albumin is 4.9, which means that it has an overall negative charge at pH ¼ 7.…”

Section: Introductionmentioning

confidence: 99%

Effect of the electrochemical characteristics of titanium on the adsorption kinetics of albumin

et al. 2019

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Structure of bovine serum albumin adsorbed on silica investigated by quartz crystal microbalance

Cited by 89 publications

References 28 publications

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

Concurrent Detection of Protein Adsorption on Mixed Nanoparticles by Differential Centrifugal Sedimentation

Effect of the electrochemical characteristics of titanium on the adsorption kinetics of albumin

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