Pre-structured hydrophobic peptide β-strands: A universal amyloid trap?

ABSTRACT: Amyloid fibril formation has long been studied because of the variety of proteins that are capable of adopting this structure despite sharing little sequence homology. This makes amyloid fibrils a challenging focus for inhibition studies because the peptides and proteins that form amyloid fibrils cannot be targeted based on a sequence motif. Most peptide inhibitors that target specific amyloidogenic proteins rely heavily on sequence recognition to ensure that the inhibitory peptide is able to bind its target. This approach is limited to targeting one amyloidogenic protein at a time. However, there is increasing evidence of cross-reactivity between amyloid-forming polypeptides. It has therefore become more useful to study the similarities between these proteins that goes beyond their sequen

SUBMITTER: Sivanesam K 

PROVIDER: S-EPMC7094768 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature