Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State.

ABSTRACT: Amyloid fibril formation is associated with several amyloidoses, including neurodegenerative Alzheimer's or Parkinson's diseases. The process of such fibrillar structure formation is still not fully understood, with new mechanistic insights appearing on a regular basis. This, in turn, has limited the development of potential anti-amyloid compounds, with only a handful of effective cures or treatment modalities available. One of the multiple amyloid aggregation factors that requires further examination is the ability of proteins to form multiple, structurally distinct aggregates, based on the environmental conditions. In this work, we examine how the initial folding state affects the fibrilization of lysozyme-an amyloidogenic protein, often used in protein aggregation studies. We show that

SUBMITTER: Mikalauskaite K 

PROVIDER: S-EPMC9141980 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature