Structural analysis of human serum albumin complexes with cationic lipids

The Journal of Physical Chemistry. B
David M CharbonneauH A Tajmir-Riahi

Abstract

Human serum albumin (HSA) is a major transporter for delivering several endogenous compounds including fatty acids in vivo. Even though HSA is the primary target of fatty acid binding, the effects of cationic lipid on protein stability and conformation have not been investigated. The aim of this study was to examine the interaction of human serum albumin (HSA) with helper lipids--cholesterol (Chol) and dioleoylphosphatidylethanolamine (DOPE)--and with cationic lipids--dioctadecyldimethylammonium bromide (DDAB) and 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP), at physiological conditions, using constant protein concentration and various lipid contents. Fourier transform infrared (FTIR), circular dichroism (CD), and fluorescence spectroscopic methods were used to analyze the lipid binding mode, the binding constant, and the effects of lipid interaction on HSA stability and conformation. Structural analysis showed that cholesterol and DOPE (helper lipids) interact mainly with HSA polypeptide polar groups and via hydrophobic moieties. Hydrophobic interactions dominate the binding of cationic lipids to HSA. The number of bound lipids (n) calculated was 1.22 (cholesterol), 1.82 (DDAB), 1.76 (DOPE), and 1.56 (DOTAP). The overall b...Continue Reading

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Citations

Nov 15, 2011·Journal of Molecular Modeling·Chandramouli MalledaRajagopal Subramanyam
Jun 22, 2011·Chemical Communications : Chem Comm·Xiaohui WangZijian Guo
Mar 24, 2012·Journal of Experimental Botany·Brandon S GueletteSusanne Hoffmann-Benning
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