University of Sussex
Browse

File(s) not publicly available

Hydrophobic, aromatic and electrostatic interactions play a central role in amyloid fibril formation

journal contribution
posted on 2023-06-08, 07:57 authored by Karen MarshallKaren Marshall, Kyle L Morris, Deborah Charlton, Nicola O’Reilly, Laurence Lewis, Helen Walden, Louise SerpellLouise Serpell
Amyloid-like fibrous crystals formed by the peptide KFFEAAAKKFFE have been previously characterized and provide an ideal model system to examine the importance of specific interactions by introducing specific substitutions. We find that the removal of any phenylalanine residue completely abrogates assembly ability, while charged residues modulate interactions within the structure resulting in alternative fibrillar morphologies. X-ray fiber diffraction analysis reveals that the essential backbone packing of the peptide molecules is maintained, while small changes accommodate differences in side chain size in the variants. We conclude that even very short peptides are adaptable and add to the growing knowledge regarding amyloid polymorphisms. Additionally, this work impacts on our understanding of the importance of residue composition for amyloidogenic peptides, in particular the roles of electrostatic, aromatic, and hydrophobic interactions in amyloid assembly.

History

Publication status

  • Published

Journal

Biochemistry

ISSN

0006-2960

Publisher

American Chemical Society

Issue

12

Volume

50

Page range

2061-2071

Department affiliated with

  • Biochemistry Publications

Notes

Corresponding author (last)

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC