Surface pressure, surface potential and ellipsometric study of cytochrome c binding to dioleoylphosphatidylcholine monolayer at the air-water interface

F. Lamarche, F. Téchy, J. Aghion, Roger Leblanc

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Abstract

The binding of soluble cytochrome c to an insoluble monolayer of dioleoylphosphatidylcholine was studied. Surface pressure, surface potential and ellipsometric isotherms show that (i) cytochrome c is not adsorbed on a phosphatidylcholine monolayer compressed at 20 mN m-1, (ii) gradual incorporation of cytochrome c takes place as surface pressure decreases, and (iii) on recompression, the adsorbed protein is desorbed from the monolayer at 14 <Π (mN m-1) < 22. In order to determine if the results can be explained by intrinsic interfacial properties of phosphatidylcholine and cytochrome c taken separately, we measured surface pressure, surface potential and ellipsometric-area isotherms of pure cytochrome c which had been (i) deposited from crystals, (ii) deposited from ethanol:H2O Solution (2:1, v/v), and (iii) adsorbed at the air-water interface after injection into the subphase. Cytochrome c behaves like an insoluble monolayer at surface pressures lower than 8-10 mN m-1 and is gradually solubilized at higher surface pressures. Then, surface pressure regulates the organization of the protein at the air-water interface and the spreading solvent does not affect its conformation. Surface potential isotherms of mixed phosphatidylcholine (18:1) -cytochrome c films compressed at different surface pressures can be explained by the simple additivity rule. We show that continuous adsorption of cytochrome c occurs when the PC (18:1) film is compressed at surface pressures lower than 8-10 mN m-1. Beyond 14 mN m-1, both surface pressure-area and ellipsometric-area isotherms demonstrate complete desorption of soluble cytochrome c from the phosphatidylcholine monolayer. The applicability of such a model system to biomembranes is discussed.

Original languageEnglish
Pages (from-to)209-222
Number of pages14
JournalColloids and Surfaces
Volume30
Issue number1
DOIs
StatePublished - Jan 1 1987
Externally publishedYes

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Surface potential
Monolayers
Proteins
Air
Water
Isotherms
Conformations
Desorption
Ethanol
Adsorption
Crystals

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Surface pressure, surface potential and ellipsometric study of cytochrome c binding to dioleoylphosphatidylcholine monolayer at the air-water interface. / Lamarche, F.; Téchy, F.; Aghion, J.; Leblanc, Roger.

In: Colloids and Surfaces, Vol. 30, No. 1, 01.01.1987, p. 209-222.

Research output: Contribution to journalArticle

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N2 - The binding of soluble cytochrome c to an insoluble monolayer of dioleoylphosphatidylcholine was studied. Surface pressure, surface potential and ellipsometric isotherms show that (i) cytochrome c is not adsorbed on a phosphatidylcholine monolayer compressed at 20 mN m-1, (ii) gradual incorporation of cytochrome c takes place as surface pressure decreases, and (iii) on recompression, the adsorbed protein is desorbed from the monolayer at 14 <Π (mN m-1) < 22. In order to determine if the results can be explained by intrinsic interfacial properties of phosphatidylcholine and cytochrome c taken separately, we measured surface pressure, surface potential and ellipsometric-area isotherms of pure cytochrome c which had been (i) deposited from crystals, (ii) deposited from ethanol:H2O Solution (2:1, v/v), and (iii) adsorbed at the air-water interface after injection into the subphase. Cytochrome c behaves like an insoluble monolayer at surface pressures lower than 8-10 mN m-1 and is gradually solubilized at higher surface pressures. Then, surface pressure regulates the organization of the protein at the air-water interface and the spreading solvent does not affect its conformation. Surface potential isotherms of mixed phosphatidylcholine (18:1) -cytochrome c films compressed at different surface pressures can be explained by the simple additivity rule. We show that continuous adsorption of cytochrome c occurs when the PC (18:1) film is compressed at surface pressures lower than 8-10 mN m-1. Beyond 14 mN m-1, both surface pressure-area and ellipsometric-area isotherms demonstrate complete desorption of soluble cytochrome c from the phosphatidylcholine monolayer. The applicability of such a model system to biomembranes is discussed.

AB - The binding of soluble cytochrome c to an insoluble monolayer of dioleoylphosphatidylcholine was studied. Surface pressure, surface potential and ellipsometric isotherms show that (i) cytochrome c is not adsorbed on a phosphatidylcholine monolayer compressed at 20 mN m-1, (ii) gradual incorporation of cytochrome c takes place as surface pressure decreases, and (iii) on recompression, the adsorbed protein is desorbed from the monolayer at 14 <Π (mN m-1) < 22. In order to determine if the results can be explained by intrinsic interfacial properties of phosphatidylcholine and cytochrome c taken separately, we measured surface pressure, surface potential and ellipsometric-area isotherms of pure cytochrome c which had been (i) deposited from crystals, (ii) deposited from ethanol:H2O Solution (2:1, v/v), and (iii) adsorbed at the air-water interface after injection into the subphase. Cytochrome c behaves like an insoluble monolayer at surface pressures lower than 8-10 mN m-1 and is gradually solubilized at higher surface pressures. Then, surface pressure regulates the organization of the protein at the air-water interface and the spreading solvent does not affect its conformation. Surface potential isotherms of mixed phosphatidylcholine (18:1) -cytochrome c films compressed at different surface pressures can be explained by the simple additivity rule. We show that continuous adsorption of cytochrome c occurs when the PC (18:1) film is compressed at surface pressures lower than 8-10 mN m-1. Beyond 14 mN m-1, both surface pressure-area and ellipsometric-area isotherms demonstrate complete desorption of soluble cytochrome c from the phosphatidylcholine monolayer. The applicability of such a model system to biomembranes is discussed.

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