Autor: |
Huihua Xing, Alison Rodger, Jeffrey Comer, Agustín S. Picco, Cristián Huck-Iriart, Edward L. Ezell, Martin Conda-Sheridan |
Rok vydání: |
2022 |
Předmět: |
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Zdroj: |
ACS applied bio materials. 5(10) |
ISSN: |
2576-6422 |
Popis: |
Hydrogen bonding plays a critical role in the self-assembly of peptide amphiphiles (PAs). Herein, we studied the effect of replacing the amide linkage between the peptide and lipid portions of the PA with a urea group, which possesses an additional hydrogen bond donor. We prepared three PAs with the peptide sequence Phe-Phe-Glu-Glu (FFEE): two are amide-linked with hydrophobic tails of different lengths and the other possesses an alkylated urea group. The differences in the self-assembled structures formed by these PAs were assessed using diverse microscopies, nuclear magnetic resonance (NMR), and dichroism techniques. We found that the urea group influences the morphology and internal arrangement of the assemblies. Molecular dynamics simulations suggest that there are about 50% more hydrogen bonds in nanostructures assembled from the urea-PA than those assembled from the other PAs. Furthermore |
Databáze: |
OpenAIRE |
Externí odkaz: |
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