Polymerization of a cysteinyl peptidolipid Langmuir film

Jianmin Xu, Changqing Li, Chengshan Wang, Jinhai Wang, Qun Huo, Roger M. Leblanc

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The surface pressure-area isotherm of a cysteinyl peptidolipid on a pure water subphase (pH 5.8) was compared with that on a water subphase saturated with oxygen and buffered with ammonium bicarbonate (pH 7.8). A reduction of the limiting molecular area was observed for the isotherm measured on the subphase saturated with oxygen. Hysteresis in the compression-decompression cycles of the Langmuir film was also observed. Taking into consideration the chemical structure of the peptidolipid, we rationalized that the free sulfhydryl groups of the peptidolipid were oxidized in the presence of oxygen in the alkaline subphase to form intermolecular disulfide bonds at the air-water interface. The surface topography of the peptidolipid Langmuir film was observed by epi-fluorescence microscopy and the Langmuir-Blodgett film by environmental scanning electron microscopy (ESEM). The micrographs showed evidence of the polymerization of the cysteinyl peptidolipid at the air-water interface. Furthermore, the XPS spectra of the Langmuir-Blodgett films also proved the existence of disulfide bonds. The control peptidolipid C 18-Ser-Gly-Ser-OH showed identical surface pressure-area isotherms in the presence or absence of an oxygen-saturated subphase.

Original languageEnglish (US)
Pages (from-to)181-186
Number of pages6
Issue number1
StatePublished - Jan 3 2006

ASJC Scopus subject areas

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


Dive into the research topics of 'Polymerization of a cysteinyl peptidolipid Langmuir film'. Together they form a unique fingerprint.

Cite this