Scanning force microscopy at the air-water interface of an air bubble coated with pulmonary surfactant

被引:30
作者
Knebel, D
Sieber, M
Reichelt, R
Galla, HJ
Amrein, M
机构
[1] Univ Munster, Inst Biochem, D-48149 Munster, Germany
[2] Univ Munster, Inst Med Phys & Biophys, D-48149 Munster, Germany
关键词
D O I
10.1016/S0006-3495(02)75412-X
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
To study the structure-function relationship of pulmonary surfactant under conditions close to nature, molecular films of a model system consisting of dipalmitoylphosphatidylcholine, dipalmitoylphosphatidylglycerol, and surfactant-associated protein C were prepared at the air-water interface of air bubbles about the size of human alveoli (diameter of 100 mum). The high mechanical stability as well as the absence of substantial film flow, inherent to small air bubbles, allowed for scanning force microscopy (SFM) directly at the air-water interface. The SFM topographical structure was correlated to the local distribution of fluorescent-labeled dipalmitoylphosphatidylcholine, as revealed from fluorescence light microscopy of the same bubbles. Although SFM has proven before to be exceptionally well suited to probe the structure of molecular films of pulmonary surfactant, the films so far had to be transferred onto a solid support from the air-water interface of a film balance, where they had been formed. This made them prone to artifacts imposed by the transfer. Moreover, the supported monolayers; disallowed the direct observation of the structural dynamics associated with expansion and compression of the films as upon breathing. The current findings are compared in this respect to our earlier findings from films, transferred onto a solid support.
引用
收藏
页码:474 / 480
页数:7
相关论文
共 31 条
[11]   Molecular structures and interactions of pulmonary surfactant components [J].
Johansson, J ;
Curstedt, T .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 244 (03) :675-693
[12]   Distribution of the surfactant-associated protein C within a lung surfactant model film investigated by near-field optical microscopy [J].
Kramer, A ;
Wintergalen, A ;
Sieber, M ;
Galla, HJ ;
Amrein, M ;
Guckenberger, R .
BIOPHYSICAL JOURNAL, 2000, 78 (01) :458-465
[13]   Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B [J].
Krol, S ;
Ross, M ;
Sieber, M ;
Künneke, S ;
Galla, HJ ;
Janshoff, A .
BIOPHYSICAL JOURNAL, 2000, 79 (02) :904-918
[14]   Structure and function of surfactant protein B and C in lipid monolayers: a scanning force microscopy study [J].
Krol, S ;
Janshoff, A ;
Ross, M ;
Galla, HJ .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2000, 2 (20) :4586-4593
[15]  
Lamb H., 1924, HYDRODYNAMICS
[16]  
Landau LD., 1991, HYDRODYNAMIK
[17]   Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence, polarized fluorescence, Brewster angle and atomic force microscopies [J].
Lee, KYC ;
Lipp, MM ;
Zasadzinski, JA ;
Waring, AJ .
LASER TECHNIQUES FOR CONDENSED-PHASE AND BIOLOGICAL SYSTEMS, 1998, 3273 :115-133
[18]   Coexistence of buckled and flat monolayers [J].
Lipp, MM ;
Lee, KYC ;
Takamoto, DY ;
Zasadzinski, JA ;
Waring, AJ .
PHYSICAL REVIEW LETTERS, 1998, 81 (08) :1650-1653
[19]   Bending rigidity of phosphatidylcholine bilayers. Dependences on experimental method, sample cell sealing and temperature [J].
Niggemann, G. ;
Kummrow, M. ;
Helfrich, W. .
Journal De Physique, II, 1995, 5 (03)
[20]   PROPERTIES, FUNCTION AND ORIGIN OF THE ALVEOLAR LINING LAYER [J].
PATTLE, RE .
NATURE, 1955, 175 (4469) :1125-1126