Intrinsic fluorescence measurements interfaces

Plasma proteins organize on polymer substrates in different ways. Adsorbates are influenced by substrate physicochemical properties and by environmental factors, especially fluid shear and bulk protein distribution. Different types of binding interactions and more than one conformation for adsorbed protein are observed. In the case of albumin, the irreversibly adsorbed conformation, as measured by pulse intrinsic fluorescence, appears to be substantially altered from that of bulk albumin. Microaggregated albumin and undenatured forms are seen at the polymer interface, which are readily desorbed by viscous drag. 

R. Homan and M. Eisenberg, A fluorescence quenching technique for the measurement of paramagnetic ion concentrations at the membrane/water interface. Intrinsic and X537A-mediated cobalt fluxes across lipid bilayer membranes, Biochim. Biophys. Acta 812, 485—4-92 (1985). 

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