Monolayer Properties of Hydrophobic α-Helical Peptides Having Various End Groups at the Air/Water Interface

Katsuhiko Fujita, Shunsaku Kimura, Yukio Imanishi, Elmar Rump, Helmut Ringsdorf

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

A hydrophobic peptide, Boc-(Ala-Aib)8-OMe (BA16M), and its end-modified derivatives were synthesized, and the pressure-area (π-A) isotherms of the peptides spread at the air/water interface were studied from the viewpoint of interhelix interactions. All π-A isotherms of the synthetic peptides showed an inflection and weak irregular bumping at a surface areas of about 240 and 230 Å2/molecule, respectively, indicating that the helix axis of the peptide is oriented parallel to the interface. A small mound was observed at around 300 Å2/molecule in the π-a isotherm of BA16M, which was ascribed to the phase transition from a liquid to a solid state. The monolayer of an equimolar mixture of the peptides having an opposite kind of charge in the end group underwent the phase transition in the π-A isotherm, which was not observed with one of the two peptides. The electrostatic interaction between the end groups should stabilize the molecular packing at the interface.

Original languageEnglish
Pages (from-to)2731-2735
Number of pages5
JournalLangmuir
Volume10
Issue number8
DOIs
Publication statusPublished - Aug 1 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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