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Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. I. Morphological Investigation

Castelletto, V.; Hamley, I. W.; Harris, P. J. F.; Olsson, Ulf LU and Spencer, N. (2009) In The Journal of Physical Chemistry Part B 113(29). p.9978-9987
Abstract
The solvent-induced transition between self-assembled structures formed by the peptide AAKLVFF is studied via electron microscopy, light scattering, and spectroscopic techniques. The peptide is based on a core fragment of the amyloid beta-peptide, KLVFF, extended by two alanine residues. AAKLVFF exhibits distinct structures of twisted fibrils in water or nanotubes in methanol. For intermediate water/methanol compositions, these structures are disrupted and replaced by wide filamentous tapes that appear to be lateral aggregates of thin protofilaments. The orientation of the beta-strands in the twisted tapes or nanotubes can be deduced from X-ray diffraction on aligned stalks, as well as FT-IR experiments in transmission compared to... (More)
The solvent-induced transition between self-assembled structures formed by the peptide AAKLVFF is studied via electron microscopy, light scattering, and spectroscopic techniques. The peptide is based on a core fragment of the amyloid beta-peptide, KLVFF, extended by two alanine residues. AAKLVFF exhibits distinct structures of twisted fibrils in water or nanotubes in methanol. For intermediate water/methanol compositions, these structures are disrupted and replaced by wide filamentous tapes that appear to be lateral aggregates of thin protofilaments. The orientation of the beta-strands in the twisted tapes or nanotubes can be deduced from X-ray diffraction on aligned stalks, as well as FT-IR experiments in transmission compared to attenuated total reflection. Strands are aligned perpendicular to the axis of the twisted fibrils or the nanotubes. The results are interpreted in light of recent results on the effect of competitive hydrogen bonding upon self-assembly in soft materials in water/methanol mixtures. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
113
issue
29
pages
9978 - 9987
publisher
The American Chemical Society
external identifiers
  • wos:000268139600044
  • scopus:67650799934
ISSN
1520-5207
DOI
10.1021/jp902860a
language
English
LU publication?
yes
id
2a48ff0f-4a6f-49dc-b7ee-86a1886aa5f7 (old id 1461495)
date added to LUP
2009-08-24 11:05:59
date last changed
2017-10-08 03:48:59
@article{2a48ff0f-4a6f-49dc-b7ee-86a1886aa5f7,
  abstract     = {The solvent-induced transition between self-assembled structures formed by the peptide AAKLVFF is studied via electron microscopy, light scattering, and spectroscopic techniques. The peptide is based on a core fragment of the amyloid beta-peptide, KLVFF, extended by two alanine residues. AAKLVFF exhibits distinct structures of twisted fibrils in water or nanotubes in methanol. For intermediate water/methanol compositions, these structures are disrupted and replaced by wide filamentous tapes that appear to be lateral aggregates of thin protofilaments. The orientation of the beta-strands in the twisted tapes or nanotubes can be deduced from X-ray diffraction on aligned stalks, as well as FT-IR experiments in transmission compared to attenuated total reflection. Strands are aligned perpendicular to the axis of the twisted fibrils or the nanotubes. The results are interpreted in light of recent results on the effect of competitive hydrogen bonding upon self-assembly in soft materials in water/methanol mixtures.},
  author       = {Castelletto, V. and Hamley, I. W. and Harris, P. J. F. and Olsson, Ulf and Spencer, N.},
  issn         = {1520-5207},
  language     = {eng},
  number       = {29},
  pages        = {9978--9987},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. I. Morphological Investigation},
  url          = {http://dx.doi.org/10.1021/jp902860a},
  volume       = {113},
  year         = {2009},
}