2020
DOI: 10.1016/j.colsurfb.2019.110604
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Conformation changes of albumin and lysozyme on electrospun TiO2 nanofibers and its effects on MSC behaviors

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Cited by 10 publications
(8 citation statements)
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“…HSA is in general a soft protein. Experimentally it was found that after immobilization or adsorption on TiO 2 surfaces [49] this soft blood protein undergoes conformational changes induced by the surface topography affecting also its tertiary structure, then the functionality [50][51][52][53][54][55][56][57][58]. These studies confirm the importance not only of the similar surface chemistry of TiO 2 surfaces but also the influence of the surface curvature on the protein-biomaterial interaction process.…”
Section: Introductionmentioning
confidence: 70%
“…HSA is in general a soft protein. Experimentally it was found that after immobilization or adsorption on TiO 2 surfaces [49] this soft blood protein undergoes conformational changes induced by the surface topography affecting also its tertiary structure, then the functionality [50][51][52][53][54][55][56][57][58]. These studies confirm the importance not only of the similar surface chemistry of TiO 2 surfaces but also the influence of the surface curvature on the protein-biomaterial interaction process.…”
Section: Introductionmentioning
confidence: 70%
“…The surface morphology, crystal structure, and surface hydroxyl groups of TiO 2 fibers can promote the adhesion and growth of MSCs on the material surface by affecting protein's adsorption and their conformational changes. 43 2.8. Osteogenic Differentiation of MSCs In Vitro.…”
Section: Migration Of Mscsmentioning
confidence: 99%
“…The extent of changes in the secondary structure of BSA was not directly correlated with the WCA of the surfaces and BSA has undergone significant conformational changes even on the hydrophilic anodized surfaces. It is generally recognized that proteins undergo less denaturation upon adsorption on hydrophilic surfaces and the restriction of protein-surface interactions due to water-surface interactions on hydrophilic TiO2 surfaces were reported to cause less denaturation compared to hydrophobic surfaces (Zhao et al, 2020). However, this conclusion doesn't take the effect of surface morphology into consideration.…”
Section: Protein Conformationmentioning
confidence: 99%
“…Rockwell et al (2012), on the other hand, reported that increased surface curvature increases protein adsorption, and Lu et al (2012) reported that increasing surface roughness between 1-11 nm increases protein adsorption due to an increase in the surface free energy (Lu et al, 2012). Zhao et al (2020) reported that upon BSA adsorption on TiO 2 nanofibers, a significant increase in β-turn and β-sheet content was observed while the random coil structure disappeared. The diameters of these structures varied between 184 ± 8 nm and 511 ± 17 nm.…”
Section: Protein Conformationmentioning
confidence: 99%
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