Theoretical study on tertiary structural elements of β-peptides

Nanotubes formed from parallel-sheet-derived assemblies of β-peptides

Tamás Beke, I. Csizmadia, A. Perczel

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30 Citations (Scopus)

Abstract

Parallel or polar strands of β-peptides spontaneously form nanotubes of different sizes in a vacuum as determined by ab initio calculations. Stability and conformational features of [CH3CO-(β-Ala) k-NHCH3]/ (1 ≤ k ≤ 4, 2 ≤ / ≤ 4) models were computed at different levels of theory (e.g., B3LYP/6-311++G(d,p)// B3LYP/6-31G(d), with consideration of BSSE). For the first time, calculations demonstrate that sheets of β-peptides display nanotubular characteristics rather than two-dimensional extended β-layers, as is the case of α-peptides. Of the configurations studied, k = / = 4 gave the most stable nanotubular structure, but larger assemblies are expected to produce even more stable nanotubes. As with other nanosystems such as cyclodextrane, these nanotubes can also incorporate small molecules, creating a diverse range of applications for these flexible, biocompatible, and highly stable molecules. The various side chains of β-peptides can make these nanosystems rather versatile. Energetic and structural features of these tubular model systems are detailed in this paper. It is hoped that the results presented in this paper will stimulate experimental research in the field of nanostructure technology involving β-peptides.

Original languageEnglish
Pages (from-to)5158-5167
Number of pages10
JournalJournal of the American Chemical Society
Volume128
Issue number15
DOIs
Publication statusPublished - Apr 19 2006

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Peptide Nanotubes
Nanotubes
Peptides
Theoretical Models
Nanosystems
Molecules
Nanostructures
Vacuum
Technology
Research

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Theoretical study on tertiary structural elements of β-peptides: Nanotubes formed from parallel-sheet-derived assemblies of β-peptides",
abstract = "Parallel or polar strands of β-peptides spontaneously form nanotubes of different sizes in a vacuum as determined by ab initio calculations. Stability and conformational features of [CH3CO-(β-Ala) k-NHCH3]/ (1 ≤ k ≤ 4, 2 ≤ / ≤ 4) models were computed at different levels of theory (e.g., B3LYP/6-311++G(d,p)// B3LYP/6-31G(d), with consideration of BSSE). For the first time, calculations demonstrate that sheets of β-peptides display nanotubular characteristics rather than two-dimensional extended β-layers, as is the case of α-peptides. Of the configurations studied, k = / = 4 gave the most stable nanotubular structure, but larger assemblies are expected to produce even more stable nanotubes. As with other nanosystems such as cyclodextrane, these nanotubes can also incorporate small molecules, creating a diverse range of applications for these flexible, biocompatible, and highly stable molecules. The various side chains of β-peptides can make these nanosystems rather versatile. Energetic and structural features of these tubular model systems are detailed in this paper. It is hoped that the results presented in this paper will stimulate experimental research in the field of nanostructure technology involving β-peptides.",
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