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• W2013124522 abstract "An interface optical technique, total internal reflection fluorescence (TIRF), permits the intrinsic tryptophan fluorescence of adsorbed proteins to be monitored continuously, in situ. The protein fluorescence emission spectrum provides information on the local tryptophan microenvironment, which can be related to the orientation and conformation of the adsorbed macromolecule. This technique has been applied to the adsorption of human plasma fibronectin on hydrophilic and hydrophobic amorphous silica surfaces. Our experiments using the TIRF technique have shown increased fibronectin binding and more rapid adsorption kinetics on hydrophobic silanized-silica in contrast to hydrophilic silica. Adsorption was essentially irreversible on both the hydrophilic and the hydrophobic surface. A 5-nm red shift in the fluorescence emission maximum occurred on the hydrophobic surface suggesting a change in protein conformation and/or microenvironment. Such behavior may correlate with changes in biological function noted by other workers. We have demonstrated that the in situ TIRF technique, utilizing intrinsic tryptophan fluorescence, is useful for probing microenvironmental effects and possibly orientation or conformational changes in adsorbed proteins. This is the first report of intrinsic TIRF fluorescence spectral changes upon adsorption." @default.
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• W2013124522 date "1985-08-01" @default.
• W2013124522 modified "2023-09-27" @default.
• W2013124522 title "Fibronectin adsorption detected by interfacial fluorescence" @default.
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• W2013124522 doi "https://doi.org/10.1016/s0021-9797(85)80020-5" @default.
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