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Originally published In Press as doi:10.1194/jlr.M400106-JLR200 on July 1, 2004

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Journal of Lipid Research, Vol. 45, 1704-1715, September 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology

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

Libo Wang and Donald M. Small1

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

1 To whom correspondence should be addressed. e-mail: dmsmall{at}bu.edu

The region between residues 968 and 1882 of apolipoprotein B (apoB-21 to apoB-41) is rich in amphipathic ß strands (AßSs) and promotes the assembly of primordial triacylglyceride (TAG)-rich lipoproteins. To understand the importance of AßS in recruiting TAG, the interfacial properties of two AßS consensus peptides, P12 and P27, were studied at dodecane/water (DD/W) and triolein/water (TO/W) interfaces. P12 (acetyl-LSLSLNADLRLK-amide) and P27 (acetyl-LSLSLNADLRLKNGNLSLSLNADLRLK-amide), when added into the aqueous phase surrounding a suspended oil drop (dodecane or triolein), decreased the interfacial tension ({gamma}) in a concentration-dependent manner. At the DD/W interface, 1 x 10–5 M P12 decreased {gamma} to ~20 mN/m and 6.6 x 10–6 M P27 decreased {gamma} to ~13 mN/m. At the TO/W interface, 1.5 x 10–5 M P12 decreased {gamma} to ~14 mN/m and 9.0 x 10–6 M P27 decreased {gamma} to ~12 mN/m. The surface area of both peptides was between 11.2 and 15.1 Å2 per residue, consistent with ß sheets 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. When P12 and P27 were compressed beyond the equilibrium {gamma} to as low as 4 mN/m, they could not be readily desorbed from either interface.

These properties probably help in assembling nascent TAG-rich lipoproteins, and AßS may anchor apoB to ß lipoproteins.

Abbreviations: AßS, amphipathic ß strand; apoB, apolipoprotein B; A/W, air/water; CSP, consensus sequence peptide, an amphipathic {alpha} helix consensus peptide derived from the water-soluble human apolipoproteins apoA-I, apoA-IV, and apoE and with the sequence (PLAEELRARLRAQLEELRERLG)2-NH2; DD/W, dodecane/water; GIXD, grazing incidence X-ray diffraction, HFIP, 1,1,1,3,3,3-hexafluoro-2-propanol; MTP, microsomal triglyceride transfer protein; PC, phosphatidylcholine; TAG, triacylglycerol; TO/W, triolein/water

Supplementary key words dodecane/water interface • triolein/water interface • air/water interface • low density lipoprotein


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