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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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Yury Velichko
Samuel I. Stupp
Mónica Olvera de la Cruz
The Journal of Physical Chemistry B
Northwestern University
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Velichko et al. (Fri,) studied this question.
www.synapsesocial.com/papers/6a0be66eaab637ffb5c21933 — DOI: https://doi.org/10.1021/jp074420n