Abstract
Gangliosides interact with human serum albumin, inducing conformational changes in its globule. Gangliosides bring about an increase in the binding constant of the fluorescent probe 1-anilinonapthalene-8-sulfonate (ANS) with model phospholipid membranes, a decrease in the rate of pyrene diffusion in liposomes. Gangliosides raise the fluorescence intensity of ANS bound with the erythrocytic membrane as the binding constant of the probe-membrane increases, the fluorescence of tryptophanils of membranous proteins gets intensified, the fluorescence maximum of ANS and tryptophan residues shifts to the short-wave area, and the accessibility of tryptophan residues for NO-3 decreases. At the same time there is a reduction in the efficacy of energy migration from tryptophan to ANS and NAD X H2. The data obtained attest to the capability of gangliosides of influencing the conformation of both the lipid and protein phases of biological membranes.
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