Study of molecular aggregation of artificial amyloid in a langmuir monolayer by infrared spectroscopy

Takeshi Hasegawa, Yoshiko Sato, Hiroyuki Kakuda, Changqing Li, Jhony Orbulescu, Roger M. Leblanc

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

A synthesized peptidolipid (C18IIGLM-NH2) comprised of a single C18-saturated hydrocarbon chain connected to the amino acid sequence IIGLM terminated with the NH2 group was spread on water, which formed a stable Langmuir monolayer. The Langmuir and Langmuir-Blodgett (LB) films have been characterized by measurements of surface pressure-area (π-A) and surface potential-area (ΔV-A) isotherms and infrared multiple-angle incidence resolution spectrometry (MAIRS). The Langmuir monolayer had a significantly larger limiting molecular area than that of a similar molecule of C18IIGLM-OH, which was reported in our previous study. The surface dipole moment analysis coupled with the π-A isotherm suggested that the C18IIGLMNH2 monolayer was extraordinarily stiff and the fundamental structure of the monolayer was brought about before the monolayer compression. The infrared MAIRS analysis of the C18IIGLM-NH 2 LB film revealed that the backbone structure of the monolayer was the 'antiparallel' β sheet aligned parallel to the substrate. Since the C18IIGLM-OH LB film was made of 'parallel' β sheet with a random orientation, it has been found that the present C18IIGLM-NH 2 Langmuir monolayer has a largely different monolayer structure, although the chemical structures are slightly different from each other by the terminal group only.

Original languageEnglish (US)
Pages (from-to)1391-1396
Number of pages6
JournalJournal of Physical Chemistry B
Volume112
Issue number5
DOIs
StatePublished - Feb 7 2008

ASJC Scopus subject areas

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

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