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Cited by 457

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Self-Assembly of Giant Peptide Nanobelts

Open access
Cui, Honggang, Muraoka, Takahiro, Cheetham, Andrew G., Stupp, Samuel I.·2009·Nano Letters

Abstract

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.

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Metadata

Authors
Cui, H., Muraoka, T., Cheetham, A. G., & Stupp, S. I.
Venue
Nano Letters
Published
2009-02-04
Volume
9
Issue
3
Pages
945-951
ISSN
  • 1530-6984 (ISSN-L)
  • 1530-6992
OpenAlex
W1997568619
Cited by
457
References
1
FWCI
12.85
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Self-Assembly of Giant Peptide Nanobelts. https://app.cochat.ai/papers/10.1021/nl802813f
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Cui, H., Muraoka, T., Cheetham, A. G., & Stupp, S. I. (2009). Self-Assembly of Giant Peptide Nanobelts. Nano Letters. https://doi.org/10.1021/nl802813f

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