Mimetic peptides of human apoA-I helix 10 get together to lower lipids and ameliorate atherosclerosis: is the action in the gut?

Geoffrey D Wool,Catherine A Reardon,Godfrey S Getz

doi:10.1194/jlr.e053538

Abstract

Mimetic peptides of human apoA-I helix 10 get together to lower lipids and ameliorate atherosclerosis: is the action in the gut?

Highlights

This issue of the Journal of Lipid Research contains an intriguing paper from the Scripps Research Institute by Zhao and colleagues [1] investigating the in vivo antiatherosclerotic properties of HDL-like nanoparticles containing α-helical amphipathic peptides
To contrast this report with the majority of work in the apoA-I mimetic peptide field, peptide mimetics such 18A and 4F have generally been investigated as monomers and administered to animals as bare peptide without associated lipid [5] with some notable exceptions [6, 7]
The improved ability of nanoparticles with peptide multimers to interact with HDL and efflux cholesterol mirrors what our group and others have reported with tandem symmetric or asymmetric dimeric apoA-I mimetic peptides with proline linkers [9,10,11]

Summary

Introduction

The Scripps group had previously shown that these nanoparticles were 9–12 nm discs that incorporated into and remodeled HDL in vitro and mediated cholesterol efflux in culture. The nanoparticles with trimeric peptides were more effective at incorporating into HDL, mediating cholesterol efflux, and were more resistant to proteolysis than the nanoparticles with monomeric peptide.

Results

Conclusion