[Modulation of Aggregation and Immunogenicity of a Protein: Based on the Study of Hen Lysozyme]

Yakugaku Zasshi. 2024;144(3):299-310. doi: 10.1248/yakushi.23-00192.
[Article in Japanese]

Abstract

This study focuses on the modulation of protein aggregation and immunogenicity. As a starting point for investigating long-range interactions within a non-native protein, the effects of perturbing denatured protein states on their aggregation, including the formation of amyloid fibrils, were evaluated. The effects of adducts, sugar modifications, and stabilization on protein aggregation were then examined. We also investigated how protein immunogenicity was affected by enhancing protein conformational stability and other factors.

Keywords: aggregation; denatured state; immunogenicity; light chain λ6; lysozyme; protein stability.

Publication types

  • English Abstract

MeSH terms

  • Muramidase*
  • Protein Aggregates*
  • Protein Conformation

Substances

  • Muramidase
  • Protein Aggregates