Abstract
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.
Highlights
The region between residues 968 and 1882 of apolipoprotein B is rich in amphipathic  strands (ASs) and promotes the assembly of primordial triacylglyceride (TAG)-rich lipoproteins
This paper looks at a consensus sequence derived from the first  sheet region of Apolipoprotein B (apoB) between apoB-21 and apoB-41 and its interaction with hydrocar
Cryoelectron microscopy images of apoB-37 and apoB-41 particles show quasi-spherical particles with an electron-lucent center consistent with a neutral lipid core [7]. It appears that the amphipathic  strands (ASs) between apoB-32 and apoB-41 are responsible for most of the recruitment of TAG in microsomal triglyceride transfer protein (MTP)-poor C-127 cells
Summary
The region between residues 968 and 1882 of apolipoprotein B (apoB-21 to apoB-41) is rich in amphipathic  strands (ASs) and promotes the assembly of primordial triacylglyceride (TAG)-rich lipoproteins. Once the interfacial tension curve approached equilibrium, the oil drop was compressed by rapidly decreasing the volume by ف12% or 25%.
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