Characterisation of the membrane affinity of an isoniazide peptide conjugate by tensiometry, atomic force microscopy and sum-frequency vibrational spectroscopy, using a phospholipid Langmuir monolayer model

Katalin Hill, Csanád Botond Pénzes, Donát Schnöller, Kata Horváti, Szilvia Bősze, Ferenc Hudecz, Tamás Keszthelyi, Éva Kiss

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Tensiometry, sum-frequency vibrational spectroscopy, and atomic force microscopy were employed to assess the cell penetration ability of a peptide conjugate of the antituberculotic agent isoniazide. Isoniazide was conjugated to peptide 91SEFAYGSFVRTVSLPV106, a functional T-cell epitope of the immunodominant 16 kDa protein of Mycobacterium tuberculosis. As a simple but versatile model of the cell membrane a phospholipid Langmuir monolayer at the liquid/air interface was used. Changes induced in the structure of the phospholipid monolayer by injection of the peptide conjugate into the subphase were followed by tensiometry and sum-frequency vibrational spectroscopy. The drug penetrated lipid films were transferred to a solid support by the Langmuir-Blodgett technique, and their structures were characterized by atomic force microscopy. Peptide conjugation was found to strongly enhance the cell penetration ability of isoniazide.

Original languageEnglish
Pages (from-to)11498-11506
Number of pages9
JournalPhysical Chemistry Chemical Physics
Volume12
Issue number37
DOIs
Publication statusPublished - Jan 1 2010

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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