Hysteresis behavior of amphiphilic model peptide in lung lipid monolayers at the air-water interface by an IRRAS measurement

Hiromichi Nakahara, Anna Dudek, Yoshihiro Nakamura, Sannamu Lee, Chien-Hsiang Chang, Osamu Shibata

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Pulmonary functions such as rapid adsorption, respreading, and hysteresis behavior of pulmonary surfactants are very important for respiratory movement. The interfacial behavior of pulmonary preparations containing an amphiphilic peptide (Hel 13-5) has recently investigated. An orientation of hydrophobic chains in a dipalmitoylphosphatidylcholine (DPPC) with or without palmitic acid (PA) is associated with a collapse of alveoli during respiration process. Therefore, the present study focused on the acyl chain orientation in model pulmonary surfactants (DPPC/Hel 13-5 and DPPC/PA/Hel 13-5). A successive change in the orientation during cyclic compression and expansion of films at the air-water interface can be probed directly by an infrared reflection-absorption spectrometry (IRRAS) technique. The hysteresis behavior, one of very important pulmonary functions, was previously observed in surface pressure (π)-molecular area (A) isotherms for the both model pulmonary surfactant systems (Langmuir 22(2006)1182-1192 and Langmuir 22(2006)5792-5803). In addition, it was reported that Hel 13-5 was squeezed-out of the surface on compression like native pulmonary surfactant proteins. The data obtained for the binary and ternary systems were compared with those of the equivalent pure DPPC and DPPC/PA mixtures, respectively. For an asymmetric methylene stretching vibration (νa-CH2) RA intensity, the absolute RA values increased with shifting to small surface area, monotonously. For the corresponding wavenumber, on the other hand, the values gradually decreased into ∼2920 cm-1. However, they were kept constant in the squeeze-out region in spite of a further decrease of surface area. These results suggested that the orientation of hydrophobic chains in DPPC and DPPC/PA mixtures became in the most packed state soon after emergence of the squeeze-out process of Hel 13-5 and then the packed orientation was retained up to the collapse state. This indicated that the squeezed-out Hel 13-5 stabilized monolayers left at the interface. For the DPPC/PA/Hel 13-5 system, in particular, dissociated PA molecules were excluded together with Hel 13-5 and the surface monolayers were refined to DPPC and undissociated PA components during the compression process. And the similar behavior in the second and third cycles supported the good respreading ability of the monolayers containing Hel 13-5.

Original languageEnglish
Pages (from-to)61-67
Number of pages7
JournalColloids and Surfaces B: Biointerfaces
Volume68
Issue number1
DOIs
Publication statusPublished - 2009 Jan 1

Fingerprint

palmitic acid
Palmitic acid
1,2-Dipalmitoylphosphatidylcholine
infrared reflection
lungs
Lipids
Spectrometry
Peptides
Palmitic Acid
peptides
Hysteresis
lipids
Monolayers
Spectrum Analysis
hysteresis
Air
Infrared radiation
Lung
Water
air

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

Cite this

Nakahara, Hiromichi ; Dudek, Anna ; Nakamura, Yoshihiro ; Lee, Sannamu ; Chang, Chien-Hsiang ; Shibata, Osamu. / Hysteresis behavior of amphiphilic model peptide in lung lipid monolayers at the air-water interface by an IRRAS measurement. In: Colloids and Surfaces B: Biointerfaces. 2009 ; Vol. 68, No. 1. pp. 61-67.
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Hysteresis behavior of amphiphilic model peptide in lung lipid monolayers at the air-water interface by an IRRAS measurement. / Nakahara, Hiromichi; Dudek, Anna; Nakamura, Yoshihiro; Lee, Sannamu; Chang, Chien-Hsiang; Shibata, Osamu.

In: Colloids and Surfaces B: Biointerfaces, Vol. 68, No. 1, 01.01.2009, p. 61-67.

Research output: Contribution to journalArticle

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T1 - Hysteresis behavior of amphiphilic model peptide in lung lipid monolayers at the air-water interface by an IRRAS measurement

AU - Nakahara, Hiromichi

AU - Dudek, Anna

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AU - Chang, Chien-Hsiang

AU - Shibata, Osamu

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AB - Pulmonary functions such as rapid adsorption, respreading, and hysteresis behavior of pulmonary surfactants are very important for respiratory movement. The interfacial behavior of pulmonary preparations containing an amphiphilic peptide (Hel 13-5) has recently investigated. An orientation of hydrophobic chains in a dipalmitoylphosphatidylcholine (DPPC) with or without palmitic acid (PA) is associated with a collapse of alveoli during respiration process. Therefore, the present study focused on the acyl chain orientation in model pulmonary surfactants (DPPC/Hel 13-5 and DPPC/PA/Hel 13-5). A successive change in the orientation during cyclic compression and expansion of films at the air-water interface can be probed directly by an infrared reflection-absorption spectrometry (IRRAS) technique. The hysteresis behavior, one of very important pulmonary functions, was previously observed in surface pressure (π)-molecular area (A) isotherms for the both model pulmonary surfactant systems (Langmuir 22(2006)1182-1192 and Langmuir 22(2006)5792-5803). In addition, it was reported that Hel 13-5 was squeezed-out of the surface on compression like native pulmonary surfactant proteins. The data obtained for the binary and ternary systems were compared with those of the equivalent pure DPPC and DPPC/PA mixtures, respectively. For an asymmetric methylene stretching vibration (νa-CH2) RA intensity, the absolute RA values increased with shifting to small surface area, monotonously. For the corresponding wavenumber, on the other hand, the values gradually decreased into ∼2920 cm-1. However, they were kept constant in the squeeze-out region in spite of a further decrease of surface area. These results suggested that the orientation of hydrophobic chains in DPPC and DPPC/PA mixtures became in the most packed state soon after emergence of the squeeze-out process of Hel 13-5 and then the packed orientation was retained up to the collapse state. This indicated that the squeezed-out Hel 13-5 stabilized monolayers left at the interface. For the DPPC/PA/Hel 13-5 system, in particular, dissociated PA molecules were excluded together with Hel 13-5 and the surface monolayers were refined to DPPC and undissociated PA components during the compression process. And the similar behavior in the second and third cycles supported the good respreading ability of the monolayers containing Hel 13-5.

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