The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

The deposition of proteins in the form of insoluble amyloid fibril aggregates is linked to a range of diseases. The supramolecular architecture of such deposits is governed by the propagation of beta-strands in the direction of protofilament growth. In the present study, we analyze the structural changes of hen egg-white lysozyme fibrils upon their interactions with a range of polysaccharides, using AFM and FTIR spectroscopy. Linear anionic polysaccharides, such as kappa-carrageenan and sodium alginate, are shown to be capable to disaggregate protofilaments with eventual protein renaturation. The results help to understand the mechanism of amyloid disaggregation and create a platform for both the development of new therapeutic agents for amyloidose treatment, and the design of novel functional protein-polysaccharide complex-based nanomaterials.

Automated summary

This study demonstrates that certain linear anionic polysaccharides have the ability to disaggregate amyloid fibrils and promote protein renaturation. These findings contribute to our understanding of the mechanism of amyloid disaggregation and provide a foundation for the development of new therapeutic agents for amyloidosis treatment and the design of novel functional protein-polysaccharide complex-based nanomaterials.