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

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

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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 SCISSORS 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 Computer Mouse 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.