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-, is...

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Bibliographic Details
Published in:Alcohol (Fayetteville, N.Y.) N.Y.), 2000-06, Vol.21 (2), p.141-147
Main Authors: Kveder, Marina, Pifat, Greta, Jelovečki, Anamarija, Klaić, Branimir, Pečar, Slavko, Schara, Milan
Format: Article
Language:English
Subjects:
1-Propanol - chemistry
1-Propanol - pharmacology
Alcoholism and acute alcohol poisoning
Alcohols
Apolipoproteins B - blood
Biological and medical sciences
Butanols - chemistry
Butanols - pharmacology
butyl alcohol
Chemical Phenomena
Chemistry, Physical
Electron Spin Resonance Spectroscopy
EPR
Ethanol - chemistry
Ethanol - pharmacology
Female
Humans
isopropyl alcohol
LDL
Lipid–protein interaction
Lipoproteins, LDL - blood
Medical sciences
Methanol - chemistry
Methanol - pharmacology
Spin Labels
Toxicology
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Summary: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.
ISSN:0741-8329
1873-6823
DOI:10.1016/S0741-8329(00)00082-3