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NMR Studies of an Exchangeable Apolipoprotein in the Lipid-bound State

EMSL Project ID


This research proposal is centered on structural studies of Manduca Sexta apolipophorin-III (apoLp-III) using a combination of nuclear magnetic resonance and molecular biology techniques. ApoLp-III serves as a model human apolipoprotein for elucidating the structural basis of apolipoprotein-lipoprotein interactions. We will particularly focus on solving the lipid-bound structure of apop-III in the apoLp-III/Preb-HDL particle, since there is no lipid-bound apolipoprotein structure available to date. We have 2H/15N/13C-triple labeled apoLp-III for 3D/4D heteronuclear NMR experiments. We have further prepared a Preb-HDL particle which contains only one apoLp-III. Unlike normal Preb-HDL which is not stable, this apoLp-III/Preb-HDL particle contains a neutral lipid core which is stable enough for 3D/4D-NMR experiments. Thus, we have solved all the technical difficulties that might hinder a NMR structural study of apoLp-III on a lipoprotein particle. We anticipate that a lipoprotein-associated structure of apoLp-III provides a biologically active conformation of human apolipoproteins for the binding to the cell surface receptors such as the LDL-receptor, or activating the lipid metabolic enzymes, such as LCAT. New knowledge of these biological processes may lead to new strategies for the therapeutic intervention in atherosclerosis and Alzheimer’s diseases.

Project Details

Project type
Capability Research
Start Date
End Date


Principal Investigator

Jianjun Wang
Wayne State University

Team Members

Jianglei Chen
Wayne State University

Bin Chen
Wayne State University

Related Publications

Chen B, X Ren, T Neville, WG Jerome, DW Hoyt, DL Sparks, G Ren, and J Wang. 2009. "Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes." Protein Science 18(5):921-935. doi:10.1002/pro.101