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Conformational studies of the lipoprotein binding domain of apolipoprotein E

Author: Arti B Patel
Publisher: [Long Beach, California] : California State University, Long Beach, 2011.
Dissertation: M.S. California State University, Long Beach 2011
Series: California State University, Long Beach.; Master's thesis collection, Dept. of Chemistry and Biochemistry.
Edition/Format:   Thesis/dissertation : Thesis/dissertation   Computer File : English
Summary:
Abstract: 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  Read more...
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Details

Genre/Form: Academic theses
Material Type: Thesis/dissertation, Internet resource
Document Type: Book, Computer File, Internet Resource
All Authors / Contributors: Arti B Patel
ISBN: 9781124994581 1124994580
OCLC Number: 1054934292
Description: xi, 97 leaves : illustrations (some color), charts
Series Title: California State University, Long Beach.; Master's thesis collection, Dept. of Chemistry and Biochemistry.
Responsibility: by Arti B. Patel.

Abstract:

Abstract: 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 [alpha]-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.

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