The EPR study of LDL perturbed by alcohols with different molecular architecture.
In this work, the interaction of different isomers of lower aliphatic alcohols with LDL representing a complex macromolecular assembly is investigated in vitro. Emphasis is given to the comparison of the impact of molecular architecture of methanol, ethanol, propanol (n-, iso-) and butanol (n-, iso-, sec-, tert-) in perturbing the lipid-protein assembly. The geometrical characteristics as well as the lipophilicity of the respective alcohol are considered. 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. In addition to the change in protein environment, the spectral decomposition of the experimental data revealed a decrease in lipid ordering with the increasing concentration of the alcohols. This phenomenon for aliphatic alcohols is linearly correlated with the equal volume occupation (EVO) 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.
Kveder
M
M
Ruder Bosković Institute, FK/LMR, Bijenicka 54, 10000 Zagreb, Croatia.
Pifat
G
G
Jelovecki
A
A
Klaić
B
B
Pecar
S
S
Schara
M
M
D000433:1-Propanol / Q000737:chemistry / Q000494:pharmacology*; D001055:Apolipoproteins B / Q000097:blood; D000440:Butanols / Q000737:chemistry / Q000494:pharmacology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004578:Electron Spin Resonance Spectroscopy; D000431:Ethanol / Q000737:chemistry / Q000494:pharmacology*; D005260:Female; D006801:Humans; D008077:Lipoproteins, LDL / Q000097:blood*; D000432:Methanol / Q000737:chemistry / Q000494:pharmacology*; D013113:Spin Labels
D001055:Apolipoproteins B; D000440:Butanols; D008077:Lipoproteins, LDL; D013113:Spin Labels; D000431:Ethanol; D000433:1-Propanol; D000432:Methanol