Structure and function of surfactant protein B and C in lipid monolayers: A scanning force microscopy study

S. Krol, A. Janshoff, M. Ross, H. J. Galla

Research output: Contribution to journalArticle

Abstract

This study focuses on the impact of surfactant protein C and B on lipid monolayers at various surface pressures. The artificial system is composed of the saturated phospholipids dipalmitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylglycerol (DPPG) in a molar ratio of 4:1 with 0.2 mol% SP-B and/or 0.4 mol% SP-C. A dominating influence of SP-C on the morphology of lipid monolayers at high surface pressure was found. Even in the presence of both proteins structural peculiarities typical for SP-C were found at elevated pressure employing tapping mode scanning force microscopy of LB-films. Stacked bilayer-protrusions known to be induced by SP-C are visible in films containing SP-C together with SP-B. The findings were corroborated by fluorescence microscopy at the air/water interface and are consistent with the appearance of the corresponding isotherms. In the low pressure regime, however, disc-like protrusions characteristic of SP-B containing films are discernible. Filamentous LE domains with large boundaries arise due to the reduced line tension in the presence of surface active proteins, particularly SP-B. Remarkably, SP-B fluidizes the monolayer to a larger extent than SP-C as revealed by scanning force microscopy images. These findings show that SP-B and SP-C interact independently of each other. Therefore we conclude that SP-C may be responsible for the fast respreading process during the breathing cycle while SP-B removes material from the monolayer in more discrete portions.

Original languageEnglish
Pages (from-to)4586-4593
Number of pages8
JournalPhysical Chemistry Chemical Physics
Volume2
Issue number20
DOIs
Publication statusPublished - Oct 15 2000

Fingerprint

Protein C
Surface-Active Agents
lipids
Monolayers
Atomic force microscopy
surfactants
microscopy
proteins
Lipids
scanning
Pulmonary Surfactant-Associated Protein B
breathing
1,2-Dipalmitoylphosphatidylcholine
Langmuir Blodgett films
Fluorescence microscopy
isotherms
low pressure
Isotherms
Phospholipids
fluorescence

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Atomic and Molecular Physics, and Optics

Cite this

Structure and function of surfactant protein B and C in lipid monolayers : A scanning force microscopy study. / Krol, S.; Janshoff, A.; Ross, M.; Galla, H. J.

In: Physical Chemistry Chemical Physics, Vol. 2, No. 20, 15.10.2000, p. 4586-4593.

Research output: Contribution to journalArticle

@article{c918dbbbed6f4af2a11d2af81edb8722,
title = "Structure and function of surfactant protein B and C in lipid monolayers: A scanning force microscopy study",
abstract = "This study focuses on the impact of surfactant protein C and B on lipid monolayers at various surface pressures. The artificial system is composed of the saturated phospholipids dipalmitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylglycerol (DPPG) in a molar ratio of 4:1 with 0.2 mol{\%} SP-B and/or 0.4 mol{\%} SP-C. A dominating influence of SP-C on the morphology of lipid monolayers at high surface pressure was found. Even in the presence of both proteins structural peculiarities typical for SP-C were found at elevated pressure employing tapping mode scanning force microscopy of LB-films. Stacked bilayer-protrusions known to be induced by SP-C are visible in films containing SP-C together with SP-B. The findings were corroborated by fluorescence microscopy at the air/water interface and are consistent with the appearance of the corresponding isotherms. In the low pressure regime, however, disc-like protrusions characteristic of SP-B containing films are discernible. Filamentous LE domains with large boundaries arise due to the reduced line tension in the presence of surface active proteins, particularly SP-B. Remarkably, SP-B fluidizes the monolayer to a larger extent than SP-C as revealed by scanning force microscopy images. These findings show that SP-B and SP-C interact independently of each other. Therefore we conclude that SP-C may be responsible for the fast respreading process during the breathing cycle while SP-B removes material from the monolayer in more discrete portions.",
author = "S. Krol and A. Janshoff and M. Ross and Galla, {H. J.}",
year = "2000",
month = "10",
day = "15",
doi = "10.1039/b004145i",
language = "English",
volume = "2",
pages = "4586--4593",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "Royal Society of Chemistry",
number = "20",

}

TY - JOUR

T1 - Structure and function of surfactant protein B and C in lipid monolayers

T2 - A scanning force microscopy study

AU - Krol, S.

AU - Janshoff, A.

AU - Ross, M.

AU - Galla, H. J.

PY - 2000/10/15

Y1 - 2000/10/15

N2 - This study focuses on the impact of surfactant protein C and B on lipid monolayers at various surface pressures. The artificial system is composed of the saturated phospholipids dipalmitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylglycerol (DPPG) in a molar ratio of 4:1 with 0.2 mol% SP-B and/or 0.4 mol% SP-C. A dominating influence of SP-C on the morphology of lipid monolayers at high surface pressure was found. Even in the presence of both proteins structural peculiarities typical for SP-C were found at elevated pressure employing tapping mode scanning force microscopy of LB-films. Stacked bilayer-protrusions known to be induced by SP-C are visible in films containing SP-C together with SP-B. The findings were corroborated by fluorescence microscopy at the air/water interface and are consistent with the appearance of the corresponding isotherms. In the low pressure regime, however, disc-like protrusions characteristic of SP-B containing films are discernible. Filamentous LE domains with large boundaries arise due to the reduced line tension in the presence of surface active proteins, particularly SP-B. Remarkably, SP-B fluidizes the monolayer to a larger extent than SP-C as revealed by scanning force microscopy images. These findings show that SP-B and SP-C interact independently of each other. Therefore we conclude that SP-C may be responsible for the fast respreading process during the breathing cycle while SP-B removes material from the monolayer in more discrete portions.

AB - This study focuses on the impact of surfactant protein C and B on lipid monolayers at various surface pressures. The artificial system is composed of the saturated phospholipids dipalmitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylglycerol (DPPG) in a molar ratio of 4:1 with 0.2 mol% SP-B and/or 0.4 mol% SP-C. A dominating influence of SP-C on the morphology of lipid monolayers at high surface pressure was found. Even in the presence of both proteins structural peculiarities typical for SP-C were found at elevated pressure employing tapping mode scanning force microscopy of LB-films. Stacked bilayer-protrusions known to be induced by SP-C are visible in films containing SP-C together with SP-B. The findings were corroborated by fluorescence microscopy at the air/water interface and are consistent with the appearance of the corresponding isotherms. In the low pressure regime, however, disc-like protrusions characteristic of SP-B containing films are discernible. Filamentous LE domains with large boundaries arise due to the reduced line tension in the presence of surface active proteins, particularly SP-B. Remarkably, SP-B fluidizes the monolayer to a larger extent than SP-C as revealed by scanning force microscopy images. These findings show that SP-B and SP-C interact independently of each other. Therefore we conclude that SP-C may be responsible for the fast respreading process during the breathing cycle while SP-B removes material from the monolayer in more discrete portions.

UR - http://www.scopus.com/inward/record.url?scp=0034667501&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034667501&partnerID=8YFLogxK

U2 - 10.1039/b004145i

DO - 10.1039/b004145i

M3 - Article

AN - SCOPUS:0034667501

VL - 2

SP - 4586

EP - 4593

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

SN - 1463-9076

IS - 20

ER -