engleski

EPR study of LDL perturbed by alcohols with different molecular architecture

The interaction of different alcohols with human plasma LDL was investigated with special emphasis on the importance of the structural properties of the alcohol molecules. The comparison of the molecular architectures of propanol (n-, iso) and butanol (n-, iso-, sec-, tert-) in perturbing the lipid-protein assembly is presented. The EPR method combined with the spin labeling of both the apoB and the lipid monolayer allowed parallel detection of changes provoked in both phases. Besides the change in protein environment, the spectral decomposition of the experimental data revealed a decrease in the lipid ordering with the increased concentration of alcohols. This phenomenon for aliphatic alcohols is linearly correlated with the equal volume occupation of alcohol in LDL. The results support the molecular mechanism of alcohol action through its interference with the lipid-protein interactions in LDL which could be applicable to the molecular mechanism of alcohol interaction with integral membrane proteins.

LDL ; EPR ; alcohols ; lipid-protein interaction

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