Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.

Abstract excerpt

A hallmark of Alzheimer's disease (AD) is the rearrangement of the β-amyloid (Aβ) peptide to a non-native conformation that promotes the formation of toxic, nanoscale aggregates. Recent studies have pointed to the role of sample preparation in creating polymorphic fibrillar species. One of many potential pathways for Aβ toxicity may be modulation of lipid membrane function on cellular surfaces. There are several...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Amyloid beta-Peptides
• Share to Amyloid Precursor Protein Secretases