Monolayers of N-stearoyltyrosine have been investigated by fluorescence microscopy and surface pressure measurements. The racemic films are more condensed than the enantiomeric films, indicating heterochiral discrimination. The surface pressure at the transition to the condensed phase on compression
Incorporation of Blood-Clotting Proteins into Phospholipid Langmuir Monolayers: A Fluorescence Microscopy Study
โ Scribed by Sam Brancato; Alexa Serfis
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 246 KB
- Volume
- 239
- Category
- Article
- ISSN
- 0021-9797
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โฆ Synopsis
Phospholipid monolayers adsorbed at an air-water interface are model cell membranes and have been used in this work to study interactions with blood-clotting proteins. Factor I (non-membrane binding) was used as a control protein, and its association with L- ฮฑ-dipalmitoylphosphatidylcholine Langmuir monolayers was compared to factor VII, a membrane-binding protein. Fluorescence micrographs indicated that factor I penetration of the lipid monolayers in the phase transition region occurred extensively, causing condensation of the lipid film. The association of factor I with phospholipid monolayers was deemed nonspecific. Factor VII was shown to associate with the periphery of lipid domains in the absence of calcium ions, causing flattening of domain edges. In the presence of calcium, factor VII induced expansion of the lipid monolayer. This effect is a specific interaction attributed to exposure of hydrophobic residues upon calcium binding, followed by protein association with lipid hydrocarbon chains.
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