Interaction of anilinonaphtyl labeled spectrin with fatty acids and phospholipids: a fluorescence study
Bonnet, D.; Begard, E.
Biochemical and Biophysical Research Communications 120(2): 344-350
1984
ISSN/ISBN: 0006-291X PMID: 6732762 Document Number: 238768
Anilinonaphthyl labeled spectrin exhibits a fluorescence emission spectrum characteristic of a highly hydrophobic environment. Quenching of the fluorescence intensity by nitroxide analogs of fatty acids of affinity 104 M-1 reveals that the sites of interaction of fatty acids lie very close to the anilinonaphtyl groups. Similar experiments performed with a nitroxide analog of phosphatidylserine yield a 30% quenching of fluorescence while the same phosphatidylcholine analog has essentially no effect. The changes in the fluorescence emission spectrum exhibited in the presence of sonicated phosphatidylserine vesicles further outline the specificity of interaction towards phosphatidylserine, with 1 spectrin binding site/.apprx. 750 exposed phospholipids. They suggest a penetration of the anilinonaphtyl group into the lipid bilayer. [The erythrocyte membrane skeleton is a proteic network underlying the plasma membrane and is involved in a number of physiologically relevant properties].