Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.

ABSTRACT: Protein fibril formation and accumulation are associated with dozens of amyloidoses, including the widespread and yet-incurable Alzheimer's and Parkinson's diseases. Currently, there are still several aspects of amyloid aggregation that are not fully understood, which negatively contributes to the development of disease-altering drugs and treatments. One factor which requires a more in-depth analysis is the effect of the environment on both the initial state of amyloidogenic proteins and their aggregation process and resulting fibril characteristics. In this work, we examine how lysozyme's folding state influences its amyloid formation kinetics and resulting aggregate structural characteristics under several different pH conditions, ranging from acidic to neutral. We demonstrate that both

SUBMITTER: Ziaunys M 

PROVIDER: S-EPMC10804668 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature