Loading…

Self-Assembly of Giant Peptide Nanobelts

Many alkylated peptide amphiphiles have been reported to self-assemble into cylindrical nanofibers with diameters on the order of a few nanometers and micrometer scale lengths; these nanostructures can be highly bioactive and are of great interest in many biomedical applications. We have discovered...

Full description

Saved in:
Bibliographic Details
Published in:Nano letters 2009-03, Vol.9 (3), p.945-951
Main Authors: Cui, Honggang, Muraoka, Takahiro, Cheetham, Andrew G, Stupp, Samuel I
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Many alkylated peptide amphiphiles have been reported to self-assemble into cylindrical nanofibers with diameters on the order of a few nanometers and micrometer scale lengths; these nanostructures can be highly bioactive and are of great interest in many biomedical applications. We have discovered the sequences for these molecules that can eliminate all curvature from the nanostructures they form in water and generate completely flat nanobelts with giant dimensions relative to previously reported systems. The nanobelts have fairly monodisperse widths on the order of 150 nm and lengths of up to 0.1 mm. The sequences have an alternating sequence with hydrophobic and hydrophilic side chains and variations in monomer concentration generate a “broom” morphology with twisted ribbons that reveals the mechanism through which giant nanobelts form. Interestingly, a variation in pH generates reversibly periodic 2 nm grooves on the surfaces of the nanobelts. With proper functionalization, these nanostructures offer a novel architecture to present epitopes to cells for therapeutic applications.
ISSN:1530-6984
1530-6992
DOI:10.1021/nl802813f