Identification of the importance of the secondary structure of Alzheimer's disease amyloid

Abstract

Studies on the nature of the interaction between the marker dye, Congo red and Alzheimer's amyloid protein have been continued. Band-decomposition methods used on the infrared spectra clarify the changes in the SO − 3 spectral region which result from dye-protein interactions and confirm the implication of this group during fixation. In order to complete a model for the mechanism of fixation, macromolecular modelling techniques have been used to obtain optimal tertiary structures of amyloid peptides 1–28 and 1–43. Finally, docking calculations indicate that arginine-5 and lysine-16 might be key residues involved in an interaction between Congo red and amyloid proteins.