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

Marshall, Karen, Morris, Kyle L, Charlton, Deborah, O’Reilly, Nicola, Lewis, Laurence, Walden, Helen and Serpell, Louise C (2011) Hydrophobic, aromatic and electrostatic interactions play a central role in amyloid fibril formation. Biochemistry, 50 (12). pp. 2061-2071. ISSN 0006-2960

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Abstract

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.

Item Type: Article
Additional Information: Corresponding author (last)
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Karen Marshall
Date Deposited: 06 Feb 2012 20:49
Last Modified: 30 Jul 2013 13:35
URI: http://sro.sussex.ac.uk/id/eprint/28318
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