Protein Conditioning for Binding Congo Red and Other Supramolecular Ligands

Abstract

Self-assembled organic compounds which form ribbon-like micellar clusters may attach themselves to proteins, penetrating in areas of low stability. Such complexation involves regions other than the protein's natural binding site. The supramolecular ligand adheres to beta folds or random coils which become susceptible to complexation as a result of function-related structural changes -e.g. antibodies engaged in immune complexes or acute phase proteins. However, even seemingly unsusceptible helical proteins may bind Congo red if they include chameleon sequences (short peptide fragments capable of adopting different secondary conformations depending on environmental conditions). Examples of such proteins include hemoglobin and albumin. Complexation of supramolecular Congo red is often associated with increased fluorescence, indicating breakdown of ligand micelles in the complex. This phenomenon may be used in diagnostic tests. Keywords

Structure and Location of Protein Sites Binding Self-Associated Congo Red Molecules with Intercalated Drugs as Compact Ligands—Theoretical Studies

“…As remarked above, the heat-modified IgG light chain reflects the structural changes which, under natural conditions, are triggered by strain associated with formation of an immune complex, where bivalent antibodies must align to randomly distributed antigen determinants. The light chain/Congo red complex, which forms under elevated temperatures, has been subjected to electrophoretic analysis, revealing limited involvement of Congo red molecules (between 4 and 8 per light chain) [ 1 , 21 , 22 , 23 , 24 , 25 , 26 ].…”