Lysine functionalised amyloid fibrils: The design and assembly of a TTR1-based peptide

Abstract

Non-core residues can affect the formation and protofilament packing of fibrils assembled from short peptide sequences. These residues are of interest in understanding amyloid diseases and in the design of self-assembling peptide materials with a cross-β core, where the assembly process should be reproducible and functional groups accessible on the fibril surface. In this study, the well characterised TTR1 peptide, also known as TTR105-115, was functionalised with glycine and lysine residues forming the peptide TTR1-GGK, with the aim of producing a self-assembling fibril scaffold that can be functionalised following assembly. A second aim was to develop a sequence capable of fibril assembly ..