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Role of apolipoprotein A-II in HDL structure-function

The question
How does apoA-II associates with HDL and how does apoA-II contribute to the regulation of HDL interaction with enzymes, and membrane receptors and transporters?

The hypothesis
Our hypothesis is that specific regions or single amino acids are essential for maintaining apoA-II native structure in the lipid-free and HDL-associated forms and preserving normal apoA-II functional levels.

The experimental approach

By mutating single amino acids or deleting entire regions in apoA-II sequence we are searching for the most important structure/function determinants of the protein. We also label apoA-II at specific positions with fluorophores to investigate how the protein self-associates and associates with HDL. Experimentally we use mutagenesis techniques and our intein-based expression and purification system to produce specific apoA-II variants. The proteins are characterized structurally by circular dichroism and fluorescence spectroscopies, and mass-spectrometry. Interaction with other proteins on HDL is investigated by fluorescence spectroscopy. The biological activity of HLD reconstituted using apoA-II variants is also evaluated using cell culture techniques.



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