This chapter discusses complexation of Congo red by amyloid structures comprising immunoglobulin light chains, particularly the so-called Bence-Jones (BJ) proteins. According to the presented study, in BJ proteins the V domain is substantially less stable than the C domain. This conclusion is based on quantitative analysis of the protein’s hydrophobic core, made possible by the fuzzy oil drop model. Results indicate that the V domain exhibits structural ordering characteristic of amyloid aggregates, i.e. linear propagation of local hydrophobicity peaks and troughs rather than a monocentric hydrophobic core (typically present in globular proteins). On this basis, the authors propose a hypothetical arrangement of V domains which leads to formation of an amyloid. Structural similarities between V domains in BJ proteins and other types of amyloid aggregates enable the authors to study the specific mechanism of Congo red complexation by amyloids.
The proposed Congo red complexation mechanism builds upon the authors’ previous experience with bioinformatics tools. The subject should be of interest to researchers specializing in protein folding studies and misfolding diseases.
Copyright 2018, The Author(s).