Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation

Abstract excerpt

Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be reflected in the aggregation mechanism. FA from different bacteria, including Escherichia coli (CsgA) and Pseudomonas (FapC), contains a number of imperfect repeats...

Topics

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

• Share to Alzheimer's disease research and treatments
• Share to Amyloidosis: Diagnosis, Treatment, Outcomes
• Share to Prion Diseases and Protein Misfolding