@article{247,
  author = {K. Hill and C. Pénzes and D. Schnöller and Kata Horváti and Szilvia Bősze and F. Hudecz and Tamás Keszthelyi and Éva Kiss},
  title = {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},
  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 (91)SEFAYGSFVRTVSLPV(106), 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.},
  year = {2010},
  journal = {Physical Chemistry Chemical Physics},
  volume = {12},
  number = {37},
  pages = {11498–11506},
  url = {http://dx.doi.org/10.1039/C002737E},
  doi = {10.1039/c002737e},
}