Protein-to-lipid ratio uniquely changes the rate of lysozyme aggregation but does not significantly alter toxicity of mature protein aggregates.

ABSTRACT: Irreversible aggregation of misfolded proteins is the underlying molecular cause of numerous pathologies, including diabetes type 2, Alzheimer's, and Parkinson's diseases. Such an abrupt protein aggregation results in the formation of small oligomers that can propagate into amyloid fibrils. A growing body of evidence suggests that protein aggregation can be uniquely altered by lipids. However, the role of the protein-to-lipid (P:L) ratio on the rate of protein aggregation, as well as the structure and toxicity of corresponding protein aggregates remains poorly understood. In this study, we investigate the role of the P:L ratio of five different phospho- and sphingolipids on the rate of lysozyme aggregation. We observed significantly different rates of lysozyme aggregation at 1:1, 1:5, and

SUBMITTER: Zhaliazka K 

PROVIDER: S-EPMC10405292 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature