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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 SerpellAmyloid-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.
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Publication status
- Published
Journal
BiochemistryISSN
0006-2960Publisher
American Chemical SocietyPublisher URL
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Issue
12Volume
50Page range
2061-2071Department affiliated with
- Biochemistry Publications
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- No
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- Yes
Legacy Posted Date
2012-02-06Usage metrics
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