Enthalpy-driven apolipoprotein A-I and lipid bilayer interaction indicating protein penetration upon lipid binding

Biochemistry
Cristina ArnulphiAna Jonas

Abstract

The interaction of lipid-free apolipoprotein A-I (apoA-I) with small unilamellar vesicles (SUVs) of 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) with and without free cholesterol (FC) was studied by isothermal titration calorimetry and circular dichroism spectroscopy. Parameters reported are the affinity constant (K(a)), the number of protein molecules bound per vesicle (n), enthalpy change (DeltaH degrees), entropy change (DeltaS degrees ), and the heat capacity change (DeltaC(p) degrees). The binding process of apoA-I to SUVs of POPC plus 0-20% (mole) FC was exothermic between 15 and 37 degrees C studied, accompanied by a small negative entropy change, making enthalpy the main driving force of the interaction. The presence of cholesterol in the vesicles increased the binding affinity and the alpha-helix content of apoA-I but lowered the number of apoA-I bound per vesicle and the enthalpy and entropy changes per bound apoA-I. Binding affinity and stoichiometry were essentially invariant of temperature for binding to SUVs of POPC/FC at a molar ratio of 6/1 at (2.8-4) x 10(6) M(-1) and 2.4 apoA-I molecules bound per vesicle or 1.4 x 10(2) phospholipids per bound apoA-I. A plot of DeltaH degrees against temperature displayed a ...Continue Reading

Citations

Aug 13, 2011·The Journal of Biological Chemistry·Shobini JayaramanGiorgio Cavigiolio
Aug 25, 2009·Journal of Lipid Research·Shobini JayaramanOlga Gursky
Mar 26, 2009·Journal of Lipid Research·Eric T AlexanderMichael C Phillips
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Apr 23, 2011·Journal of Molecular Biology·Lionel ChièzeVéronique Vié
Nov 3, 2010·Biochimica Et Biophysica Acta·Masafumi TanakaHiroyuki Saito
Apr 26, 2005·Biophysical Journal·Cristina ArnulphiAna Jonas
Nov 29, 2005·Archives of Biochemistry and Biophysics·Weimin ZhangDonald F Becker
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