| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 69: 974-988 (1995)
© 1995 the Biophysical Society
Département de Chimie, Université Laval, Quebec, Canada.
ABSTRACT
The interaction of a nonspecific wheat lipid transfer protein (LTP) with phospholipids has been studied using the monolayer technique as a simplified model of biological membranes. The molecular organization of the LTP-phospholipid monolayer has been determined by using polarized attenuated total internal reflectance infrared spectroscopy, and detailed information on the microstructure of the mixed films has been investigated by using epifluorescence microscopy. The results show that the incorporation of wheat LTP within the lipid monolayers is surface-pressure dependent. When LTP is injected into the subphase under a dipalmytoylphosphatidylglycerol monolayer at low surface pressure (< 20 mN/m), insertion of the protein within the lipid monolayer leads to an expansion of dipalmytoylphosphatidylglycerol surface area. This incorporation leads to a decrease in the conformational order of the lipid acyl chains and results in an increase in the size of the solid lipid domains, suggesting that LTP penetrates both expanded and solid domains. By contrast, when the protein is injected under the lipid at high surface pressure (> or = 20 mN/m) the presence of LTP leads neither to an increase of molecular area nor to a change of the lipid order, even though some protein molecules are bound to the surface of the monolayer, which leads to an increase of the exposure of the lipid ester groups to the aqueous environment. On the other hand, the conformation of LTP, as well as the orientation of alpha-helices, is surface-pressure dependent. At low surface pressure, the alpha-helices inserted into the monolayers are rather parallel to the monolayer plane. In contrast, at high surface pressure, the alpha-helices bound to the surface of the monolayers are neither parallel nor perpendicular to the interface but in an oblique orientation.
This article has been cited by other articles:
![]() |
H. Gaussier, T. Lefevre, and M. Subirade Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization Appl. Envir. Microbiol., November 1, 2003; 69(11): 6777 - 6784. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Dubreil, V. Vie, S. Beaufils, D. Marion, and A. Renault Aggregation of Puroindoline in Phospholipid Monolayers Spread at the Air-Liquid Interface Biophys. J., October 1, 2003; 85(4): 2650 - 2660. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. M. Eklund and J. Edqvist Localization of Nonspecific Lipid Transfer Proteins Correlate with Programmed Cell Death Responses during Endosperm Degradation in Euphorbia lagascae Seedlings Plant Physiology, July 1, 2003; 132(3): 1249 - 1259. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Söderlund, J. Y. A. Lehtonen, and P. K. J. Kinnunen Interactions of Cyclosporin A with Phospholipid Membranes: Effect of Cholesterol Mol. Pharmacol., January 1, 1999; 55(1): 32 - 38. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |