Dissertation/Thesis Abstract

Antimicrobial and lipid binding properties of the C-terminal domain of apolipoprotein A-I determined using a novel apolipophorin III/apolipoprotein A-I (179-243) chimera
by Ellena, Rachel A, M.S., California State University, Long Beach, 2016, 117; 10144827
Abstract (Summary)

Apolipoprotein A-I (apoA-I) is an exchangeable apolipoprotein that constitutes the major protein component of high density cholesterol. ApoA-I is a two-domain protein comprising an N-terminal helix bundle and a less-structured C-terminal domain in the lipid-free state. In the present study, the contribution of the C-terminal domain to the lipid binding and antimicrobial activity of apoA-I was investigated using a chimeric construct in which the C-terminal domain of apoA-I (179-243) was attached to an insect apolipoprotein, Locusta migratoria apolipophorin III (apoLp-III), bearing cysteine substitutions for residues 20 and 149. Circular dichroism results were consistent with the addition of a poorly structured domain to apoLp-III and revealed the apoLp-III helix bundle was successfully closed under oxidizing conditions. Electrophoresis, fluorescence spectroscopy and an in vitro study using macrophage cells revealed that the C-terminal domain in itself was insufficient for efficient binding to lipid, lipopolysaccharide and phosphatidylglycerol vesicles. These results suggest the underlying mechanisms governing these interactions are potentiated by cooperativity between the N- and C-terminal domains of apoA-I.

Indexing (document details)
Advisor: Weers, Paul
Commitee: Narayanaswami, Vasanthy, Schwans, Jason
School: California State University, Long Beach
Department: Chemistry and Biochemistry
School Location: United States -- California
Source: MAI 56/01M(E), Masters Abstracts International
Subjects: Biochemistry
Keywords: Apolipoprotein A-I, C-terminal domain, High density cholesterol
Publication Number: 10144827
ISBN: 978-1-369-00407-6
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