Abstract
Changes of human serum albumin (HSA) and gamma globulins (γG), labelled with 1-pyrene-carboxaldehyde (PCA) and/or with 1,3-bis(1- pyrene)-propane (BPP), resulting from interactions with polystyrene (PS) and poly(styrene/acrolein) (PSA) latexes, were investigated by fluorescence spectros copy. The proteins in solution readily exchanged with the adsorbed proteins. The fluorescence spectra of the PCA label and BPP probe, incorporated into the protein macromolecules, indicate that the protein macromolecules undergo sig nificant conformational changes on contact with the surface of the latex par ticles, and that these changes are not reversible. The internal fluidity for desorbed protein macromolecules is lower than before the interaction with the latex particles. Moreover, due to the conformational changes the PCA labels, formerly present in the hydrophilic and hydrophobic protein regions, became located predominantly in the latter. The differences in the emission spectra for the labelled proteins before attachment to the latex particles and after desorp tion were used to study the kinetics of the protein conformational changes. The dependence of the overall rate constants for protein conformational rearrange ments on the latex concentration was investigated.
Get full access to this article
View all access options for this article.