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Cited by 218

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Molecular Simulation Study of Peptide Amphiphile Self-Assembly

Velichko, Yuri S., Stupp, Samuel I., de la Cruz, Monica Olvera·2008·The Journal of Physical Chemistry B

Abstract

We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single beta-sheets connected laterally by hydrogen bonds, stacks of parallel beta-sheets, spherical micelles, micelles with beta-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.

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Metadata

Authors
Velichko, Y. S., Stupp, S. I., & de la Cruz, M. O.
Venue
The Journal of Physical Chemistry B
Published
2008-02-01
Volume
112
Issue
8
Pages
2326-2334
ISSN
  • 1520-5207 (ISSN-L)
  • 1520-6106
OpenAlex
W2043110985
Cited by
218
References
1
FWCI
5.45
Type
journal article
Language
en
Open access
closed

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