In the past two decades, amyloids, typically associated with human diseases, have been
described to play various functional roles in nearly all life forms. The structural and functional …

Protein aggregation and amyloid formation have historically been linked with various
diseases such as Alzheimer's and Parkinson's disease, but recently functional amyloids …

Functional amyloid (FAs), particularly the bacterial proteins CsgA and FapC, have many
useful properties as biomaterials: high stability, efficient, and controllable formation of a …

Biofilm-protected pathogenic Staphylococcus aureus causes chronic infections that are
difficult to treat. An essential building block of these biofilms are functional amyloid fibrils that …

Protein domains without the usual distribution of amino acids, called low complexity (LC)
domains, can be prone to self-assembly into amyloid-like fibrils. Self-assembly of LC …

Bacterial functional amyloids contribute to biofilm development by bacteria and provide
protection from the immune system and prevent antibiotic treatment. Strategies to target …

A commercially available small-angle X-ray scattering (SAXS) NanoSTAR instrument
(Bruker AXS) with a liquid-metal-jet source (Excillum) has been optimized for solution …

The need to develop new antimicrobial peptides is due to the high resistance of pathogenic
bacteria to traditional antibiotics now and in the future. The creation of synthetic peptide …

Functional bacterial amyloids (FuBA) are intrinsically disordered proteins (IDPs) which
rapidly and efficiently aggregate, forming extremely stable fibrils. The conversion from IDP to …

Proteins and their aggregation is significant field of research due to their association with
various conformational maladies including well-known neurodegenerative diseases like …