Polymerization of a cysteinyl peptidolipid Langmuir film

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

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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
Pages (from-to)181-186
Number of pages6
JournalLangmuir
Volume22
Issue number1
DOIs
StatePublished - Jan 3 2006

Fingerprint

Langmuir Blodgett films
polymerization
Polymerization
Oxygen
Isotherms
isotherms
Water
disulfides
oxygen
Langmuir-Blodgett films
Disulfides
water
Ammonium bicarbonate
Fluorescence microscopy
air
pressure reduction
Surface topography
Air
Hysteresis
carbonates

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Polymerization of a cysteinyl peptidolipid Langmuir film. / Xu, Jianmin; Li, Changqing; Wang, Chengshan; Wang, Jinhai; Huo, Qun; Leblanc, Roger.

In: Langmuir, Vol. 22, No. 1, 03.01.2006, p. 181-186.

Research output: Contribution to journalArticle

Xu, J, Li, C, Wang, C, Wang, J, Huo, Q & Leblanc, R 2006, 'Polymerization of a cysteinyl peptidolipid Langmuir film', Langmuir, vol. 22, no. 1, pp. 181-186. https://doi.org/10.1021/la0527700
Xu, Jianmin ; Li, Changqing ; Wang, Chengshan ; Wang, Jinhai ; Huo, Qun ; Leblanc, Roger. / Polymerization of a cysteinyl peptidolipid Langmuir film. In: Langmuir. 2006 ; Vol. 22, No. 1. pp. 181-186.
@article{c8aaa3b9066540c2872f2f12566ec0b8,
title = "Polymerization of a cysteinyl peptidolipid Langmuir film",
abstract = "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.",
author = "Jianmin Xu and Changqing Li and Chengshan Wang and Jinhai Wang and Qun Huo and Roger Leblanc",
year = "2006",
month = "1",
day = "3",
doi = "10.1021/la0527700",
language = "English",
volume = "22",
pages = "181--186",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "1",

}

TY - JOUR

T1 - Polymerization of a cysteinyl peptidolipid Langmuir film

AU - Xu, Jianmin

AU - Li, Changqing

AU - Wang, Chengshan

AU - Wang, Jinhai

AU - Huo, Qun

AU - Leblanc, Roger

PY - 2006/1/3

Y1 - 2006/1/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=30344470492&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=30344470492&partnerID=8YFLogxK

U2 - 10.1021/la0527700

DO - 10.1021/la0527700

M3 - Article

C2 - 16378418

AN - SCOPUS:30344470492

VL - 22

SP - 181

EP - 186

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 1

ER -