Highly stable pleated-sheet secondary structure in assemblies of amphiphilic α/β-peptides at the air-water interface

Shlomit Segman, Myung Ryul Lee, Vladimir Vaiser, Samuel H. Gellman, Hanna Rapaport

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

(Figure Presented) A nice gathering at the interface: The de novo design and characterization of amphiphilic α/β-peptides, which form ordered two-dimensional assemblies at the air-water interface composed of olig-omers in pleated conformation similar to β-sheets of a-peptides, is reported. The positioning of ionic side chains along the backbone can exert a profound effect on the propensity to self-assemble.

Original languageEnglish
Pages (from-to)716-719
Number of pages4
JournalAngewandte Chemie - International Edition
Volume49
Issue number4
DOIs
StatePublished - 18 Jan 2010

Keywords

  • Foldamers
  • Monolayers
  • Peptides
  • Self-assembly
  • β-sheet

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