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M507657200v1
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Papers In Press, published online ahead of print January 3, 2006
J. Biol. Chem, 10.1074/jbc.M507657200
Submitted on July 14, 2005
Revised on December 7, 2005
Accepted on January 3, 2006

Self-association and lipid binding properties of the lipoprotein initiating domain of apolipoprotein B

Aubrey S. Ledford, Richard B. Weinberg, Victoria R. Cook, Roy R. Hantgan, and Gregory S. Shelness

Dept. of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1040

Corresponding Author: gshelnes{at}wfubmc.edu

The amino-terminal 20.1% of apolipoprotein B (apoB20.1; residues 1-912) is sufficient to initiate and direct the formation of nascent apoB-containing lipoprotein particles. To investigate the mechanism of initial lipid acquisition by apoB, we examined the lipid binding and interfacial properties of a C-terminal His6-tagged form of apoB20.1 (apoB20.1H). ApoB20.1H was expressed in Sf9 cells and purified by nickel affinity chromatography. ApoB20.1H was produced in a folded state, characterized by formation of intramolecular disulfide bonds and resistance to chemical reduction. Dynamic light scattering in physiological buffer indicated that purified apoB20.1H forms multimers, which were readily dissociable upon addition of nonionic detergent (0.1% Triton X-100). ApoB20.1H was incapable of binding dimyristoylphosphatidylcholine multilamellar vesicles, unless its multimeric structure was first disrupted by guanidine hydrochloride. However, apoB20.1H multimers spontaneously dissociated and bound to the interface of naked and phospholipid-coated triolein microdroplets. These data reveal that the initiating domain of apoB contains solvent accessible hydrophobic sequences, which, in the absence of a hydrophobic lipid interface or detergent, engage in self-association. The high affinity of apoB20.1H for neutral lipid is consistent with the membrane binding and desorption model of apoB-containing lipoprotein assembly.


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