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Papers In Press, published online ahead of print July 1, 2004
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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
Revised on June 16, 2004
Accepted on June 17, 2004
Interfacial properties of amphipathic
strand consensus peptides of apolipoprotein B at oil/water interfaces
strands (AS) and promotes the assembly with lipids to form a primordial triglyceride (TAG) rich lipoprotein particle. To understand the importance of AS in recruiting lipids, e.g. TAG, the interfacial properties of two AS 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 AS 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 (
) in a concentration dependant fashion. At DD/W interface, 1x10-5M P12 lowered to ~20mN/m, and 6.6x10-6M P27 lowered to ~13mN/m. At TO/W interface, 1.5x10-5M P12 lowered to ~14mN/m and 9.0x10-6M P27 lowered 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 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 AS may anchor apoB to the surface of beta lipoproteins.
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