1983
DOI: 10.1016/0021-9797(83)90113-3
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Interaction of fibrinogen with solid surfaces of varying charge and hydrophobic—hydrophilic balance

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Cited by 125 publications
(55 citation statements)
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“…11,[54][55][56] We and others previously suggested that most fibrinogen molecules are oriented vertically on the surface when immobilized at high density and horizontally at low density. [57][58][59][60] Thus, on high-density fibrinogen, the ␣IIb␤3 recognition sites on the ␥-chain C-termini are likely to extend out from the surface, whereas on low-density fibrinogen the horizontal orientation is likely to reduce access to the ␥-chain C-termini and/or induce conformational changes by multiple contacts between fibrinogen molecules and the surface. This may expose regions that are cryptic in solution [61][62][63] and make them available for the interaction with the integrin, maybe contributing to the unique outside-in signaling observed on low-density fibrinogen.…”
Section: Discussionmentioning
confidence: 99%
“…11,[54][55][56] We and others previously suggested that most fibrinogen molecules are oriented vertically on the surface when immobilized at high density and horizontally at low density. [57][58][59][60] Thus, on high-density fibrinogen, the ␣IIb␤3 recognition sites on the ␥-chain C-termini are likely to extend out from the surface, whereas on low-density fibrinogen the horizontal orientation is likely to reduce access to the ␥-chain C-termini and/or induce conformational changes by multiple contacts between fibrinogen molecules and the surface. This may expose regions that are cryptic in solution [61][62][63] and make them available for the interaction with the integrin, maybe contributing to the unique outside-in signaling observed on low-density fibrinogen.…”
Section: Discussionmentioning
confidence: 99%
“…It was concluded that iodination as well as fluorescamine labeling can influence chromatographic and electrophoretic properties. (27)(28)(29)(30)(31)41) have reported that no effect of the presence of a label on the adsorption of proteins onto different surfaces was found. A possible preferential adsorption was determined by carrying out protein adsorption studies with a constant bulk protein concentration and a variation in the percentage of labeled protein.…”
Section: Discussionmentioning
confidence: 99%
“…Thus, the adsorption of fibrinogen on PDMAEMA, and to some extent also on PSPMA, can be associated with attractive electrostatic interactions (though this does not explain why adsorption is higher on the nominally neutral PHEMA-co-PEG10MA than on the zwitterionic PSBMA). Early studies on the adsorption of fibrinogen on various polyelectrolyte surfaces also demonstrated high adsorption (from concentrations > 0.5 mg/mL) on those which have bulk ionexchange capacities of +0.8 meq g -1 (Schmitt et al 1983). The presence of deprotonated and hydrophobic segments in PDMAEMA at pH 7.4 might also contribute to a higher adsorption via hydrophobic interactions.…”
Section: Fouling Assaysmentioning
confidence: 99%