Structural and functional characterization of human apolipoprotein E 72-166 peptides in both aqueous and lipid environments.

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 ma

SUBMITTER: Hsieh YH 

PROVIDER: S-EPMC3022805 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature