Apolipoprotein E (apoE) is crucial for lipid/cholesterol transport in the plasma and brain. The C-terminal domain (CT) of apoE is involved in high-affinity lipoprotein binding and bears self-association sites. The high-resolution structure of the CT (residues 201-299) or intact protein is mostly unknown. To gain insights into the conformation of isolated CT, we employed site-specific fluorescence analysis by probing positions predicted to be in the non-helical (209), and class A (223 or 255) or class G* (277) amphipathic α-helices. Our studies infer that the entire apoE CT self-associates via helix-helix interactions in a parallel orientation. Also we suggest that the C-terminal G* helix of apoE likely initiates binding to lipoproteins. We propose that parallel orientated apoE CT dimers circumscribe the periphery of nascent high density lipoproteins. Structural analysis of a 26 residue peptide, ATI-5261 based on apoE CT revealed features for enhancing mimetic peptide stability and therapeutic properties.
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 50/03M, Masters Abstracts International|
|Subjects:||Molecular biology, Biochemistry, Biophysics|
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