The contrasting effect of macromolecular crowding on amyloid fibril formation.

ABSTRACT:

Background

Amyloid fibrils associated with neurodegenerative diseases can be considered biologically relevant failures of cellular quality control mechanisms. It is known that in vivo human Tau protein, human prion protein, and human copper, zinc superoxide dismutase (SOD1) have the tendency to form fibril deposits in a variety of tissues and they are associated with different neurodegenerative diseases, while rabbit prion protein and hen egg white lysozyme do not readily form fibrils and are unlikely to cause neurodegenerative diseases. In this study, we have investigated the contrasting effect of macromolecular crowding on fibril formation of different proteins.

Methodology/principal findings

As revealed by assays based on thioflavin T binding and turbidity, human Tau frag

SUBMITTER: Ma Q 

PROVIDER: S-EPMC3340346 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature