Albumin-lysozyme interactions: Cooperative adsorption on titanium and enzymatic activity

Rösch, Christina; Kratz, Fabian; Hering, T.; Trautmann, Simone; Umanskaya, Natalia; Tippkötter, N.; Müller‐Renno, Christine; Ulber, Roland; Ziegler, Christiane

doi:10.1016/j.colsurfb.2016.09.048

Cited by 12 publications

(5 citation statements)

References 37 publications

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“…Different protein solutions were prepared using physiological saline (pH 7.0-7.2) as a solvent, including 0.01 mg/mL, 0.02 mg/mL, 0.03 mg/mL, 0.04 mg/mL, and 0.05 mg/mL under room temperature and measured at a wavelength (λ) of 205 nm [29]. The measured absorbance values vs. protein concentrations calibrated by a BCA assay [30] were noted to construct the standard calibration curve.…”

Section: Protein Adsorption Areal Density Measurementmentioning

confidence: 99%

Correlation between Tribological Properties and the Quantified Structural Changes of Lysozyme on Poly (2-hydroxyethyl methacrylate) Contact Lens

Chang

et al. 2020

Polymers

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The ocular discomfort is the leading cause of contact lens wear discontinuation. Although the tear proteins as a lubricant might improve contact lens adaptation, some in vitro studies suggested that the amount of adsorbed proteins could not simply explain the lubricating performance of adsorbed proteins. The purpose of this study was to quantify the structural changes and corresponding ocular lubricating properties of adsorbed protein on a conventional contact lens material, poly (2-hydroxyethyl methacrylate) (pHEMA). The adsorption behaviors of lysozyme on pHEMA were determined by the combined effects of protein–surface and protein–protein interactions. Lysozyme, the most abundant protein in tear, was first adsorbed onto the pHEMA surface under widely varying protein solution concentrations to saturate the surface, with the areal density of the adsorbed protein presenting different protein–protein effects within the layer. These values were correlated with the measured secondary structures, and corresponding friction coefficient of the adsorbed and protein covered lens surface, respectively. The decreased friction coefficient value was an indicator of the lubricated surfaces with improved adaptation. Our results indicate that the protein–protein effects help stabilize the structure of adsorbed lysozyme on pHEMA with the raised friction coefficient measured critical for the innovation of contact lens material designs with improved adaptation.

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Section: Protein Adsorption Areal Density Measurementmentioning

confidence: 99%

Correlation between Tribological Properties and the Quantified Structural Changes of Lysozyme on Poly (2-hydroxyethyl methacrylate) Contact Lens

Chang

et al. 2020

Polymers

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“…Relative amounts of adsorbed proteins are influenced both by solution composition and pH, as possible to see in Figure 10a,b. Interestingly, residual enzymatic activity of LYS is not much influenced on protein content in solution [222]. BSA, due to its larger mass, cannot be displaced by LYS in case of sequential adsorption, thus limiting LYS amount on the surface [223].…”

Section: Protein Co-adsorption and Competition For The Surfacementioning

confidence: 99%

Biomaterials in Bone Tissue Engineering

Wang¹,

Lee²,

Zhao³

et al. 2019

Materials Science and Technology

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“…Adsorption of BSA on cp-Ti was found to be enhanced when obtained from BSA-LYS containing solutions [222,223]. BSA -LYS + agglomerates can form in solution and adsorb on the surface, thus increasing the total mass of adsorbed proteins (Figure 10).…”

Section: Protein Co-adsorption and Competition For The Surfacementioning

confidence: 99%

“…Materials 2021, 14,222 However, there is no scientific literature reporting on the effect of distribution of bone metabolism on bone graft healing characteristics of already well-integrated bone graft.…”

Section: Conflicts Of Interestmentioning

confidence: 99%