2015
DOI: 10.1016/j.colsurfb.2015.06.009
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Protein covalent immobilization via its scarce thiol versus abundant amine groups: Effect on orientation, cell binding domain exposure and conformational lability

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Cited by 23 publications
(20 citation statements)
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“…As described in Fig. 1, the amino groups (lysyl moieties) of FN can react with active ester functions present on the surfaces, while its sulfhydryl groups (cysteyl moieties) enable a reaction with maleimidyl groups on the surfaces [37,[49][50][51]. The successful grafting of the eight crosslinkers and subsequently of FN was confirmed by X-ray Photo-electron Spectroscopy (XPS), contact angle measurements, and Atomic Force Microscopy (AFM).…”
Section: Introductionmentioning
confidence: 87%
“…As described in Fig. 1, the amino groups (lysyl moieties) of FN can react with active ester functions present on the surfaces, while its sulfhydryl groups (cysteyl moieties) enable a reaction with maleimidyl groups on the surfaces [37,[49][50][51]. The successful grafting of the eight crosslinkers and subsequently of FN was confirmed by X-ray Photo-electron Spectroscopy (XPS), contact angle measurements, and Atomic Force Microscopy (AFM).…”
Section: Introductionmentioning
confidence: 87%
“…A study by Ba et al covalently anchored fibronectin via reactions through thiols or primary amines on amine-functionalized polystyrene in an attempt to restrict the orientation of fibronectin on the surface. These reactions increased the retention of fibronectin to the surface, resulting in higher amounts of immobilized fibronectin and a resistance to deformation, but did not increase the availability of binding sites [24]. Klotzsch et al used single-molecule imaging of fibronectin to track the relative distance between four available cysteines labeled with Cy3B and tracked using photobleaching and total internal reflectance spectroscopy.…”
Section: Biological Functionalizationmentioning
confidence: 99%
“…However, enzymes may encounter structural change upon immobilization due to protein conformation change at the interface, resulting in a reduction of their biocatalytic activity. There are many factors involved in enzyme conformational changes including the features of enzyme molecules and the support material (size and topography), systematic conditions (e.g., pH and temperature) as well as interaction forces (e.g., polar or hydrophobic/hydrophilic) [4][5][6]. The functionality and stability of the immobilized enzymes in a bioreactor system remain a major challenge in large scale operation.…”
Section: Introductionmentioning
confidence: 99%