Hen egg lysozyme fibrils act as amyloid nucleating agents for β-lactoglobulin and insulin
Abstract
stable non-covalent interactions dominated by H-bonds and hydrophobic contacts. Our data clearly demonstrate that the cross-β structure of lysozyme can trap native structures of both insulin and β-lactoglobulin; however, the marginally higher affinity for the monomers of β-lactoglobulin resulted in faster kinetics of the cross-seeding reactions. At the monomeric level, we also observed a rapid coaggregation process for heteromeric combinations of these proteins. The results signify that amyloid cross-seeding/coaggregation could be central to the mechanism for the formation of heterogenous amyloid structures and targeting cross-seeding and coaggregation may help in developing better anti-amyloid strategies.
Fields of Study & Subjects
Alzheimer's disease research and treatments
Prion Diseases and Protein Misfolding
Protein purification and stability
Publication details
- Journal / source
- Journal of Materials Chemistry B
- Volume
- 14
- Issue
- 15
- Pages
- 4613–4623
- Publication date
- 1 January 2026
- Language
- EN