Shear Alignment of Bola-Amphiphilic Arginine-Coated Peptide Nanotubes

Tutkimustuotos: Lehtiartikkeli

Tutkijat

  • Ian W. Hamley
  • Samuel Burholt
  • Jessica Hutchinson
  • Valeria Castelletto
  • Emerson Rodrigo da Silva
  • Wendel Alves
  • Philipp Gutfreund
  • Lionel Porcar
  • Rajeev Dattani
  • Daniel Hermida-Merino
  • Gemma Newby
  • Mehedi Reza
  • Janne Ruokolainen

  • Joanna Stasiak

Organisaatiot

  • ESRF European Synchrotron, European Synchrotron Radiation Facility (ESRF)
  • University of Reading
  • Universidade Federal do ABC
  • Institut Laue-Langevin
  • University of Cambridge

Kuvaus

The bola-amphiphilic arginine-capped peptide RFL4RF self-assembles into nanotubes in aqueous solution. The nanostructure and rheology are probed by in situ simultaneous rheology/small-angle scattering experiments including rheo-SAXS, rheo-SANS, and rheo-GISANS (SAXS: small-angle X-ray scattering, SANS: small-angle neutron scattering, GISANS: grazing incidence small-angle neutron scattering). Nematic alignment of peptide nanotubes under shear is observed at sufficiently high shear rates under steady shear in either Couette or cone-and-plate geometry. The extent of alignment increases with shear rate. A shear plateau is observed in a flow curve measured in the Couette geometry, indicating the presence of shear banding above the shear rate at which significant orientation is observed (0.1-1 s(-1)). The orientation under shear is transient and is lost as soon as shear is stopped. GISANS shows that alignment at the surface of a cone-and-plate cell develops at sufficiently high shear rates, very similar to that observed in the bulk using the Couette geometry. A small isotope effect (comparing H2O/D2O solvents) is noted in the CD spectra indicating increased interpeptide hydrogen bonding in D2O, although this does not influence nanotube self-assembly. These results provide new insights into the controlled alignment of peptide nanotubes for future applications.

Yksityiskohdat

AlkuperäiskieliEnglanti
Sivut141-149
Sivumäärä9
JulkaisuBiomacromolecules
Vuosikerta18
Numero1
TilaJulkaistu - tammikuuta 2017
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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