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Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. I. Morphological investigation.

DOI: 10.1021/jp902860a DOI Help
PMID: 19555054 PMID Help

Authors: Valeria Castelletto (University of Reading) , Ian Hamley (University of Reading, Diamond Light Source) , P. Harris (University of Reading) , U Olsson (Uinversity of Reading) , N Spencer (University of Reading)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Physical Chemistry B , VOL 113 (29) , PAGES 9978-9987

State: Published (Approved)
Published: July 2009

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.

Subject Areas: Chemistry

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