aalto1 untyped-item.component.html
Shear Alignment of Bola-Amphiphilic Arginine-Coated Peptide Nanotubes
Loading...
Access rights
openAccess
publishedVersion
URL
Journal Title
Journal ISSN
Volume Title
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
This publication is imported from Aalto University research portal.
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
Unless otherwise stated, all rights belong to the author. You may download, display and print this publication for Your own personal use. Commercial use is prohibited.
Date
Department
Major/Subject
Mcode
Degree programme
Language
en
Pages
9
Series
Biomacromolecules, Volume 18, issue 1, pp. 141-149
Abstract
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.
Description
Keywords
Other note
Citation
Hamley, I W, Burholt, S, Hutchinson, J, Castelletto, V, da Silva, E R, Alves, W, Gutfreund, P, Porcar, L, Dattani, R, Hermida-Merino, D, Newby, G, Reza, M, Ruokolainen, J & Stasiak, J 2017, 'Shear Alignment of Bola-Amphiphilic Arginine-Coated Peptide Nanotubes', Biomacromolecules, vol. 18, no. 1, pp. 141-149. https://doi.org/10.1021/acs.biomac.6b01425