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Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability
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Marshall, Karen E., 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 and stability. Biochemistry, 50 (12). pp. 2061-2071. doi:10.1021/bi101936c
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Official URL: http://dx.doi.org/10.1021/bi101936c
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: | Journal Article | ||||||
|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QP Physiology | ||||||
| Divisions: | Faculty of Science > Life Sciences (2010- ) | ||||||
| Library of Congress Subject Headings (LCSH): | Peptides -- Molecular aspects -- Research, Amyloid | ||||||
| Journal or Publication Title: | Biochemistry | ||||||
| Publisher: | American Chemical Society | ||||||
| ISSN: | 0006-2960 | ||||||
| Official Date: | 2011 | ||||||
| Dates: |
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| Volume: | 50 | ||||||
| Number: | 12 | ||||||
| Number of Pages: | 10 | ||||||
| Page Range: | pp. 2061-2071 | ||||||
| DOI: | 10.1021/bi101936c | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Restricted or Subscription Access | ||||||
| Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Alzheimer Research Trust (Great Britain) (ART) |
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