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

The region between residues 968 and 1882 of apolipoprotein B (apoB-21 to apoB-41) is rich in amphipathic beta strands (AbetaSs) and promotes the assembly of primordial triacylglyceride (TAG)-rich lipoproteins. To understand the importance of AbetaS in recruiting TAG, the interfacial properties of two AbetaS 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 approximately 20 mN/m and 6.6 x 10(-6) M P27 decreased gamma to approximately 13 mN/m. At the TO/W interface, 1.5 x 10(-5) M P12 decreased gamma to approximately 14 mN/m and 9.0 x 10(-6) M P27 decreased gamma to approximately 12 mN/m. The surface area of both peptides was between 11.2 and 15.1 angstroms2 per residue, consistent with beta 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 AbetaS may anchor apoB to beta lipoproteins. Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.