Protein adsorption mechanisms at rough surfaces: Serum albumin at a gold substrate

Adamczyk, Zbǐgniew; Pomorska, Agata; Nattich-Rak, Małgorzata; Wytrwał-Sarna, Magdalena; Bernasik, Andrzej

doi:10.1016/j.jcis.2018.06.063

Cited by 44 publications

(60 citation statements)

References 31 publications

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“…These disadvantages can be partially eliminated applying the quartz crystal microbalance (QCM) technique that enables versatile, real-time studies of protein adsorption and desorption kinetics on various substrates in liquid phases under flow conditions. − ,,− Because of exceptional sensitivity, this method is also used to study the kinetics of nanoparticle and microparticle deposition on various substrates. − …”

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confidence: 99%

Hydrodynamic Solvent Coupling Effects in Quartz Crystal Microbalance Measurements of Nanoparticle Deposition Kinetics

Adamczyk

Sadowska

2020

Anal. Chem.

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Hydrodynamic coupling effects pertinent to quartz crystal microbalance (QCM) investigation of nanoparticle adsorption kinetics were evaluated using atomic force microscopy and the theoretical modeling. Monodisperse polymer particles of the size between 26 and 140 nm and the density of 1.05 g cm –3 were used. The ζ-potential of particles was opposite to the substrate ζ-potential that promoted their irreversible adsorption on the silica sensor. The experimental kinetic data were interpreted in terms of theoretical calculations derived from the hybrid random sequential adsorption model. This allowed us to determine the amount of hydrodynamically coupled solvent (electrolyte) for the absolute particle coverage range up to 0.5. The coupling function representing the ratio of the solvent to the particle volumes was also determined and used to explicitly calculate the solvent level in particle monolayers. It is shown that the solvent level abruptly increases with the particle coverage attaining values comparable with the particle size. One can expect that these results can serve as useful reference data for the interpretation of protein adsorption kinetics on rough surfaces where the presence of stagnant solvent is inevitable.

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confidence: 99%

Hydrodynamic Solvent Coupling Effects in Quartz Crystal Microbalance Measurements of Nanoparticle Deposition Kinetics

Adamczyk

Sadowska

2020

Anal. Chem.

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“…For comparison, in the case of albumin (HSA) adsorption at the silica sensor, the hydration function in the limit of low coverage was equal to 0.65 at pH 3.5 and 0.01 M NaCl concentration [ 42 ]. Given that the hydrodynamic diameter of the myoglobin molecule equal to 4.1 nm it is much smaller than the one of the HSA molecule, equal to 7.9 nm [ 43 ] the lower value of the hydration function can be attributed to the sensor roughness effect discussed in ref. [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

“…Given that the hydrodynamic diameter of the myoglobin molecule equal to 4.1 nm it is much smaller than the one of the HSA molecule, equal to 7.9 nm [ 43 ] the lower value of the hydration function can be attributed to the sensor roughness effect discussed in ref. [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

“…Using the above estimated value of the hydration function, one can calculate from Equation (3) that the dry coverage of irreversibly bound myoglobin is equal to 0.60 ± 0.1 mg m −2 (at 0.01 M NaCl and a pH of 3.5–4). It is interesting to mention that for albumin (HSA) the coverage was equal to 0.7 mg m −2 under the same pH and NaCl concentration [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

“…It is interesting to mention that similar values of K a = 1.2 cm and

equal to −17.8 kT were previously determined in ref. [ 43 ] for the human serum albumin (HSA) desorption from silica sensor (at pH 3.5, 0.01 M NaCl concentration) applying an exact solution of the mass transfer equation.…”

Section: Resultsmentioning

confidence: 99%

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Mechanism of Myoglobin Molecule Adsorption on Silica: QCM, OWLS and AFM Investigations

Wasilewska

Nattich-Rak

Pomorska

et al. 2021

IJERPH

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Adsorption kinetics of myoglobin on silica was investigated using the quartz crystal microbalance (QCM) and the optical waveguide light-mode spectroscopy (OWLS). Measurements were carried out for the NaCl concentration of 0.01 M and 0.15 M. A quantitative analysis of the kinetic adsorption and desorption runs acquired from QCM enabled the maximum coverage of irreversibly bound myoglobin molecules to be determined. At a pH of 3.5–4 this was equal to 0.60 mg m−2 and 1.3 mg m−2 for a NaCl concentration of 0.01 M and 0.15 M, respectively, which agrees with the OWLS measurements. The latter value corresponds to the closely packed monolayer of molecules predicted from the random sequential adsorption approach. The fraction of reversibly bound protein molecules and their biding energy were also determined. It is observed that at larger pHs, the myoglobin adsorption kinetics was much slower. This behavior was attributed to the vanishing net charge that decreased the binding energy of molecules with the substrate. Beside significance to basic science, these results enabled us to develop a procedure for preparing myoglobin layers at silica substrates of well-controlled coverage that can be used for biosensing purposes.

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Effect of Hydroxyapatite Coating Surface Morphology on Adsorption Behavior of Differently Charged Proteins

Sun

Deng

2020

J Bionic Eng

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Protein adsorption mechanisms at rough surfaces: Serum albumin at a gold substrate

Cited by 44 publications

References 31 publications

Hydrodynamic Solvent Coupling Effects in Quartz Crystal Microbalance Measurements of Nanoparticle Deposition Kinetics

Hydrodynamic Solvent Coupling Effects in Quartz Crystal Microbalance Measurements of Nanoparticle Deposition Kinetics

Mechanism of Myoglobin Molecule Adsorption on Silica: QCM, OWLS and AFM Investigations

Effect of Hydroxyapatite Coating Surface Morphology on Adsorption Behavior of Differently Charged Proteins

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