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J. Lipid Res.
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A more recent version of this article appeared on September 1, 2004

Papers In Press, published online ahead of print July 1, 2004
J. Lipid Res., doi:10.1194/jlr.M400106-JLR200
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Submitted on March 16, 2004
Revised on June 16, 2004
Accepted on June 17, 2004

Interfacial properties of amphipathic beta strand consensus peptides of apolipoprotein B at oil/water interfaces

Libo Wang and Donald M. Small

Department of Physiology and Biophysics, Boston University, Boston, MA 02118

Corresponding Author: dmsmall{at}bu.edu

The region between amino acid residue 968 and 1882 of apolipoprotein B (apoB21 – apoB41) are rich in amphipathic beta strands (Abeta S) and promotes the assembly with lipids to form a primordial triglyceride (TAG) rich lipoprotein particle. To understand the importance of Abeta S in recruiting lipids, e.g. TAG, the interfacial properties of two Abeta S consensus peptides, P12 and P27 were studied using an oil-drop tensiometer at dodecane/water (DD/W) and triolein/water (TO/W) interfaces. P12 (Ac-LSLSLNADLRLK-amide) and P27 (Ac- LSLSLNADLRLKNGNLSLSLNADLRLK-amide) contain a consensus sequence (-LSLSLNADLRLK-) of Abeta S common to both apoB21-apoB41 and apoB32-apoB41. Both P12 and P27, when added into the aqueous phase surrounding a suspended oil drop (dodecane or triolein), lowered the interfacial tension (gamma ) in a concentration dependant fashion. At DD/W interface, 1x10-5M P12 lowered gamma to ~20mN/m, and 6.6x10-6M P27 lowered gamma to ~13mN/m. At TO/W interface, 1.5x10-5M P12 lowered gamma to ~14mN/m and 9.0x10-6M P27 lowered gamma to ~12mN/m, respectively. The surface area per P12 molecule was estimated 144Å2 on DD/W and 181Å2 on TO/W, while that of P27 was 268Å2 on DD/W and 280Å2 on TO/W. Those areas (11.2 to 15.1 Å2 per residue) are consistent with the adsorbed P12 and P27 lying flat on DD/W and TO/W interfaces. P12 and P27 are almost purely elastic on DD/W, TO/W and air/water interfaces with very small phase angles (<8 deg.). When P12 and P27 were compressed beyond the equilibrium gamma to as low as 4mN/m, bound peptides could not be readily desorbed from either interface. These properties may play a critical role in the assembly of the nascent TAG-rich lipoprotein and such Abeta S may anchor apoB to the surface of beta lipoproteins.


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