Peptide nanotubes self-assembled from leucine-rich alpha helical surfactant-like peptides

[thumbnail of Open access]
Preview
Text (Open access) - Published Version
· Available under License Creative Commons Attribution Non-commercial.
· Please see our End User Agreement before downloading.
| Preview
[thumbnail of L12R3ChemCommRevisedTracked.pdf]
Text - Accepted Version
· Restricted to Repository staff only
Restricted to Repository staff only

Please see our End User Agreement.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

Add to AnyAdd to TwitterAdd to FacebookAdd to LinkedinAdd to PinterestAdd to Email

Castelletto, V., Seitsonen, J., Ruokolainen, J., Piras, C., Cramer, R. orcid id iconORCID: https://orcid.org/0000-0002-8037-2511, Edwards-Gayle, C. J. C. and Hamley, I. W. orcid id iconORCID: https://orcid.org/0000-0002-4549-0926 (2020) Peptide nanotubes self-assembled from leucine-rich alpha helical surfactant-like peptides. Chemical Communications, 56 (80). pp. 11977-11980. ISSN 1359-7345 doi: 10.1039/D0CC04299D

Abstract/Summary

The designed arginine-rich surfactant-like peptide R3L12 (arginine3–leucine12) is shown to form a remarkable diversity of self-assembled nanostructures in aqueous solution, depending on pH, including nanotubes, mesh-like tubular networks in three-dimensions and square planar arrays in two-dimensions. These structures are built from α-helical antiparallel coiled–coil peptide dimers arranged perpendicular to the nanotube axis, in a “cross-α” nanotube structure. The aggregation behavior is rationalized based on the effects of dimensionality, and the balance of hydrophobic and electrostatic interactions. The nanotube and nanomesh structures display arginine at high density on their surfaces, which may be valuable for future applications.

Altmetric Badge

Item Type Article
URI https://reading-clone.eprints-hosting.org/id/eprint/92606
Identification Number/DOI 10.1039/D0CC04299D
Refereed Yes
Divisions Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher Royal Society of Chemistry
Download/View statistics View download statistics for this item

Downloads

Downloads per month over past year

University Staff: Request a correction | Centaur Editors: Update this record

Search Google Scholar