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Self-Assembly of Peptide Nanotubes in an Organic Solvent

DOI: 10.1021/la800942n DOI Help
PMID: 18572891 PMID Help

Authors: M. J. Krysmann (University of Reading) , V. Castelletto (University of Reading) , J. E. Mckendrick (University of Reading) , L. A. Clifton (University of Reading) , P. J. F. Harris (University of Reading) , I. W. Hamley (Diamond Light Source) , S. M. King (Rutherford Appleton Laboratory)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Langmuir , VOL 24 (15) , PAGES 8158-8162

State: Published (Approved)
Published: August 2008

Abstract: The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence A beta(16-20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.

Subject Areas: Chemistry, Materials


Instruments: NONE-No attached Diamond beamline

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