Amyloid formation of mutated Alzheimer's Aβ 16-36 residues peptide and application in toxic lead and uranium ion binding.

ABSTRACT: Amyloid nanostructures are gaining attention as bio-compatible materials with diverse potential applications. The formation/self-assembly of amyloid fibrils, though implicated in the prognosis of several neurodegenerative diseases, contrastingly can also be explored for their functional properties owing to their unique stability and strength. The physicochemical environment and amino-acid composition are characteristic and specifically crucial for a protein/peptide to form amyloid fibrils. The Aβ peptide involved in the Alzheimer's disease prognosis consists of two central hydrophobic core regions and a central polar region forming a β-hairpin. In this study, a 21 amino acid containing peptide KLVFFAEDVESNRGAIIGLMV is designed introducing point mutations to the original 16-36 residues of t

SUBMITTER: Natarajan A 

PROVIDER: S-EPMC12395192 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature