Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. I. Morphological Investigation
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1461495
- author
- Castelletto, V. ; Hamley, I. W. ; Harris, P. J. F. ; Olsson, Ulf LU and Spencer, N.
- organization
- publishing date
- 2009
- 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 (ACS)
- external identifiers
-
- wos:000268139600044
- scopus:67650799934
- pmid:19555054
- 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
- 2016-04-01 13:12:20
- date last changed
- 2022-03-21 17:17:12
@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 (ACS)}}, 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}}, doi = {{10.1021/jp902860a}}, volume = {{113}}, year = {{2009}}, }