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

Olga N MakshakovaLiliya BogdanovaDzhigangir A FaizullinDiliara KhaibrakhmanovaSufia ZiganshinaElena ErmakovaYuriy F ZuevIgor A Sedov
Published in: Pharmaceutics (2023)
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 β-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 κ-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.
Keyphrases
  • water soluble
  • protein protein
  • amino acid
  • binding protein
  • high resolution
  • single molecule
  • atomic force microscopy
  • replacement therapy
  • neural network