Dynamic surface activity of films of lung surfactant phospholipids, hydrophobic proteins, and neutral lipids

Z. Wang, Stephen (Steve) Hall, R. H. Notter

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

Surface pressure area (Π-A) isotherms during dynamic cycling were measured for films of dipalmitoyl phosphatidylcholine (DPPC) and column- separated fractions of calf lung surfactant extract (CLSE). Emphasis was on defining the relative importance of lung surfactant phospholipids (PPL), neutral lipids (N), and hydrophobic proteins (SP) in facilitating dynamic respreading and surface tension lowering within the interfacial film itself. Solvent-spread films in a Wilhelmy balance were studied at 23° and 37°C over a range of cycling rates for initial concentrations giving both monomolecular and surface-excess films. A striking finding was that PPL films containing the complete mix of surfactant phospholipids had greatly improved dynamic respreading corn, pared to DPPC, particularly surface excess films (30 and 15 Å 2/molecule). Hydrophobic gave an additional increase in dynamic respreading in SP and PL compared to PPL films for initial concentrations of 60, 30, and 15 Å 2/molecule. Neutral lipids also improved respreading slightly in N and PL versus PPL films, but maximum surface pressures in N and PL films at 37°C were consistently the lowest of any surfactant subtraction. Spread films of SP and PL at 60 and 30 Å 2/molecule had lower maximum pressures than PPL, but maximum pressures were slightly larger for SP and PL films at high initial concentration (15 Å 2/molecule). Supplementary oscillating bubble studies involving both adsorption and film dynamics at rapid cycling rate (20 cycles/min) showed that dispersions of CLSE and SP and PL lowered surface tension to

Original languageEnglish (US)
Pages (from-to)1283-1293
Number of pages11
JournalJournal of Lipid Research
Volume36
Issue number6
StatePublished - 1995
Externally publishedYes

Fingerprint

Motion Pictures
Surface-Active Agents
Phospholipids
Lipids
Lung
Pressure
1,2-Dipalmitoylphosphatidylcholine
Proteins
Surface Tension
Molecules
Adsorption
Zea mays
Surface tension
Dispersions
Isotherms

Keywords

  • apolipoproteins
  • interfacial films
  • surface pressure
  • surface tension

ASJC Scopus subject areas

  • Endocrinology

Cite this

Dynamic surface activity of films of lung surfactant phospholipids, hydrophobic proteins, and neutral lipids. / Wang, Z.; Hall, Stephen (Steve); Notter, R. H.

In: Journal of Lipid Research, Vol. 36, No. 6, 1995, p. 1283-1293.

Research output: Contribution to journalArticle

@article{37a1b2a0739f4aff9202af8b92c8a5ea,
title = "Dynamic surface activity of films of lung surfactant phospholipids, hydrophobic proteins, and neutral lipids",
abstract = "Surface pressure area (Π-A) isotherms during dynamic cycling were measured for films of dipalmitoyl phosphatidylcholine (DPPC) and column- separated fractions of calf lung surfactant extract (CLSE). Emphasis was on defining the relative importance of lung surfactant phospholipids (PPL), neutral lipids (N), and hydrophobic proteins (SP) in facilitating dynamic respreading and surface tension lowering within the interfacial film itself. Solvent-spread films in a Wilhelmy balance were studied at 23° and 37°C over a range of cycling rates for initial concentrations giving both monomolecular and surface-excess films. A striking finding was that PPL films containing the complete mix of surfactant phospholipids had greatly improved dynamic respreading corn, pared to DPPC, particularly surface excess films (30 and 15 {\AA} 2/molecule). Hydrophobic gave an additional increase in dynamic respreading in SP and PL compared to PPL films for initial concentrations of 60, 30, and 15 {\AA} 2/molecule. Neutral lipids also improved respreading slightly in N and PL versus PPL films, but maximum surface pressures in N and PL films at 37°C were consistently the lowest of any surfactant subtraction. Spread films of SP and PL at 60 and 30 {\AA} 2/molecule had lower maximum pressures than PPL, but maximum pressures were slightly larger for SP and PL films at high initial concentration (15 {\AA} 2/molecule). Supplementary oscillating bubble studies involving both adsorption and film dynamics at rapid cycling rate (20 cycles/min) showed that dispersions of CLSE and SP and PL lowered surface tension to",
keywords = "apolipoproteins, interfacial films, surface pressure, surface tension",
author = "Z. Wang and Hall, {Stephen (Steve)} and Notter, {R. H.}",
year = "1995",
language = "English (US)",
volume = "36",
pages = "1283--1293",
journal = "Journal of Lipid Research",
issn = "0022-2275",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "6",

}

TY - JOUR

T1 - Dynamic surface activity of films of lung surfactant phospholipids, hydrophobic proteins, and neutral lipids

AU - Wang, Z.

AU - Hall, Stephen (Steve)

AU - Notter, R. H.

PY - 1995

Y1 - 1995

N2 - Surface pressure area (Π-A) isotherms during dynamic cycling were measured for films of dipalmitoyl phosphatidylcholine (DPPC) and column- separated fractions of calf lung surfactant extract (CLSE). Emphasis was on defining the relative importance of lung surfactant phospholipids (PPL), neutral lipids (N), and hydrophobic proteins (SP) in facilitating dynamic respreading and surface tension lowering within the interfacial film itself. Solvent-spread films in a Wilhelmy balance were studied at 23° and 37°C over a range of cycling rates for initial concentrations giving both monomolecular and surface-excess films. A striking finding was that PPL films containing the complete mix of surfactant phospholipids had greatly improved dynamic respreading corn, pared to DPPC, particularly surface excess films (30 and 15 Å 2/molecule). Hydrophobic gave an additional increase in dynamic respreading in SP and PL compared to PPL films for initial concentrations of 60, 30, and 15 Å 2/molecule. Neutral lipids also improved respreading slightly in N and PL versus PPL films, but maximum surface pressures in N and PL films at 37°C were consistently the lowest of any surfactant subtraction. Spread films of SP and PL at 60 and 30 Å 2/molecule had lower maximum pressures than PPL, but maximum pressures were slightly larger for SP and PL films at high initial concentration (15 Å 2/molecule). Supplementary oscillating bubble studies involving both adsorption and film dynamics at rapid cycling rate (20 cycles/min) showed that dispersions of CLSE and SP and PL lowered surface tension to

AB - Surface pressure area (Π-A) isotherms during dynamic cycling were measured for films of dipalmitoyl phosphatidylcholine (DPPC) and column- separated fractions of calf lung surfactant extract (CLSE). Emphasis was on defining the relative importance of lung surfactant phospholipids (PPL), neutral lipids (N), and hydrophobic proteins (SP) in facilitating dynamic respreading and surface tension lowering within the interfacial film itself. Solvent-spread films in a Wilhelmy balance were studied at 23° and 37°C over a range of cycling rates for initial concentrations giving both monomolecular and surface-excess films. A striking finding was that PPL films containing the complete mix of surfactant phospholipids had greatly improved dynamic respreading corn, pared to DPPC, particularly surface excess films (30 and 15 Å 2/molecule). Hydrophobic gave an additional increase in dynamic respreading in SP and PL compared to PPL films for initial concentrations of 60, 30, and 15 Å 2/molecule. Neutral lipids also improved respreading slightly in N and PL versus PPL films, but maximum surface pressures in N and PL films at 37°C were consistently the lowest of any surfactant subtraction. Spread films of SP and PL at 60 and 30 Å 2/molecule had lower maximum pressures than PPL, but maximum pressures were slightly larger for SP and PL films at high initial concentration (15 Å 2/molecule). Supplementary oscillating bubble studies involving both adsorption and film dynamics at rapid cycling rate (20 cycles/min) showed that dispersions of CLSE and SP and PL lowered surface tension to

KW - apolipoproteins

KW - interfacial films

KW - surface pressure

KW - surface tension

UR - http://www.scopus.com/inward/record.url?scp=0028997966&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028997966&partnerID=8YFLogxK

M3 - Article

VL - 36

SP - 1283

EP - 1293

JO - Journal of Lipid Research

JF - Journal of Lipid Research

SN - 0022-2275

IS - 6

ER -