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Biophysical Journal 16: 1297-1314 (1976)
© 1976 the Biophysical Society

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The interaction of the polyene antibiotic lucensomycin with cholesterol in erythrocyte membranes and in model systems. III. Characterization of spectral parameters.

R Strom, W E Blumberg, R E Dale and C Crifo

ABSTRACT

The variations of optical density and fluorescence of lucensomycin are good indices of the binding of this polyenic antibiotic to membranes. The former parameter reflects more generally the binding to any site present in the membrane, while the latter is more specific for binding to cholesterol. The chromophore of the lucensomycin-cholesterol complex has a relatively long lifetime, is almost immobile in the membrane, and is not accessible to water-soluble fluorescence-quenching agents. The stoichiometry, evaluated fluorometrically, corresponds to about two cholesterol molecules per polyene. In colloidal cholesterol suspensions, the extent of binding as a function of free polyene concentration is described by rectangular hyperbolae, the dissociation constant being, however, dependent on the sterol concentration. In erythrocyte membranes, on the other hand, and even more markedly in model systems containing appropriate solvents, the combination between lucensomycin and the sterol sites is described by sigmoid titration curves, indicative of cooperative effects, and probably due to solvation of cholesterol.




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A. Coutinho and M. Prieto
Cooperative Partition Model of Nystatin Interaction with Phospholipid Vesicles
Biophys. J., May 1, 2003; 84(5): 3061 - 3078.
[Abstract] [Full Text] [PDF]


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