Inhibition of aggregation of a biomimic peptidolipid langmuir monolayer by congo red studied by UV-vis and infrared spectroscopies

Takeshi Hasegawa, Yoshiko Sato, Tetsuo Okada, Masami Shibukawa, Changqing Li, Jhony Orbulescu, Roger M. Leblanc

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2 Scopus citations

Abstract

A synthetic peptidolipid consisted of a hydrocarbon chain with a chain length of C18 and a peptide moiety of IIGLM terminated with an amine group, designated as C18IIGLM-NH2, has been employed as a biomimic model compound of amyloid peptide for exploring molecular interaction and orientation with the use of the Langmuir monolayer and Langmuir-Blodgett film techniques. Inspired by a well-known fact that a stain reagent, Congo red (CR), binds well to the amyloid-mimic part (IIGLM), inhibition of molecular aggregation of C18IIGLM-NH2 by interaction with CR was expected, and it has been investigated by use of surface pressure-area isotherm, surface dipole moment-area isotherm, Brewster-angle microscopy, and UV-vis/ infrared spectroscopies. It has been revealed that monomelic CR molecules whose long axis is parallel to the Langmuir monolayer surface are penetrating the C18IIGLM-NH2 Langmuir monolayer, which plays a role of inhibition of molecular aggregation via hydrogen bonding.

Original languageEnglish (US)
Pages (from-to)14227-14232
Number of pages6
JournalJournal of Physical Chemistry B
Volume111
Issue number51
DOIs
StatePublished - Dec 27 2007

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ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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