Secondary structure dependent self-assembly of β-peptides into nanosized fibrils and membranes

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84 Citations (Scopus)

Abstract

(Figure Presented) In control: The secondary structure dependent self-assembly of β-peptides in solution proves that natural biopolymers are not unique in their highly structured conformational behavior. Stereochemically controlled secondary structural units of β-peptide strands and helices intrinsically self-associate into pleated-sheet sandwiches (see picture) and helix-bundle membranes, respectively.

Original languageEnglish
Pages (from-to)2396-2400
Number of pages5
JournalAngewandte Chemie - International Edition
Volume45
Issue number15
DOIs
Publication statusPublished - Apr 3 2006

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Self assembly
Peptides
Membranes
Biopolymers

Keywords

  • Beta-peptides
  • Foldamers
  • Nanomaterials
  • Peptide mimetics
  • Self-assembly

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Secondary structure dependent self-assembly of β-peptides into nanosized fibrils and membranes",
abstract = "(Figure Presented) In control: The secondary structure dependent self-assembly of β-peptides in solution proves that natural biopolymers are not unique in their highly structured conformational behavior. Stereochemically controlled secondary structural units of β-peptide strands and helices intrinsically self-associate into pleated-sheet sandwiches (see picture) and helix-bundle membranes, respectively.",
keywords = "Beta-peptides, Foldamers, Nanomaterials, Peptide mimetics, Self-assembly",
author = "T. Martinek and A. Het{\'e}nyi and L. F{\"u}l{\"o}p and I. M{\'a}ndity and G. T{\'o}th and I. D{\'e}k{\'a}ny and F. F{\"u}l{\"o}p",
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T1 - Secondary structure dependent self-assembly of β-peptides into nanosized fibrils and membranes

AU - Martinek, T.

AU - Hetényi, A.

AU - Fülöp, L.

AU - Mándity, I.

AU - Tóth, G.

AU - Dékány, I.

AU - Fülöp, F.

PY - 2006/4/3

Y1 - 2006/4/3

N2 - (Figure Presented) In control: The secondary structure dependent self-assembly of β-peptides in solution proves that natural biopolymers are not unique in their highly structured conformational behavior. Stereochemically controlled secondary structural units of β-peptide strands and helices intrinsically self-associate into pleated-sheet sandwiches (see picture) and helix-bundle membranes, respectively.

AB - (Figure Presented) In control: The secondary structure dependent self-assembly of β-peptides in solution proves that natural biopolymers are not unique in their highly structured conformational behavior. Stereochemically controlled secondary structural units of β-peptide strands and helices intrinsically self-associate into pleated-sheet sandwiches (see picture) and helix-bundle membranes, respectively.

KW - Beta-peptides

KW - Foldamers

KW - Nanomaterials

KW - Peptide mimetics

KW - Self-assembly

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SN - 1433-7851

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