Dataset Information
Structural and functional characterization of human apolipoprotein E 72-166 peptides in both aqueous and lipid environments.
Ontology highlight
ABSTRACT: Backgrounds
There are three apolipoprotein E (apoE) isoforms involved in human lipid homeostasis. In the present study, truncated apoE2-, apoE3- and apoE4-(72-166) peptides that are tailored to lack domain interactions are expressed and elucidated the structural and functional consequences.Methods & results
Circular dichroism analyses indicated that their secondary structure is still well organized. Analytical ultracentrifugation analyses demonstrated that apoE-(72-166) produces more complicated species in PBS. All three isoforms were significantly dissociated in the presence of dihexanoylphosphatidylcholine. Dimyristoylphosphatidylcholine turbidity clearance assay showed that apoE4-(72-166) maintains the highest lipid-binding capacity. Finally, only apoE4-(72-166) still maintained significant LDL receptor binding ability.Conclusions
Overall, apoE4-(72-166) peptides displayed a higher lipid-binding and comparable receptor-binding ability as to full-length apoE. These findings provide the explanation of diverged functionality of truncated apoE isoforms.
SUBMITTER: Hsieh YH
PROVIDER: S-EPMC3022805 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Publications
Structural and functional characterization of human apolipoprotein E 72-166 peptides in both aqueous and lipid environments.
Journal of biomedical science 20110110
<h4>Backgrounds</h4>There are three apolipoprotein E (apoE) isoforms involved in human lipid homeostasis. In the present study, truncated apoE2-, apoE3- and apoE4-(72-166) peptides that are tailored to lack domain interactions are expressed and elucidated the structural and functional consequences.<h4>Methods & results</h4>Circular dichroism analyses indicated that their secondary structure is still well organized. Analytical ultracentrifugation analyses demonstrated that apoE-(72-166) produces ...[more]
