Institutional members access full text with Ovid®

Share this article on:

The structure/function of apoprotein A-I mimetic peptides: an update

Getz, Godfrey S.; Reardon, Catherine A.

Current Opinion in Endocrinology, Diabetes and Obesity: April 2014 - Volume 21 - Issue 2 - p 129–133
doi: 10.1097/MED.0000000000000045
LIPIDS: Edited by Annabelle Rodriguez

Purpose of review To review recent advances in our understanding of the mechanism of action of apoprotein A-I (apoA-I) mimetic peptides and improved methods for the oral delivery of peptides.

Recent findings The apoA-I mimetic peptides are based on the structure of the major apoprotein of HDL with the expectation that they may also mimic some of the antiatherogenic functions of HDL. Recent work has provided insight into mechanisms by which they may be antioxidative and anti-inflammatory. In addition, recent work has shifted the focus of the site of action of the mimetic peptides to the small intestine from the plasma and HDL and suggests modulation of bioactive oxidized lipids in the intestine by the peptides may be a major antiatherogenic pathway. The development of transgenic tomatoes expressing an apoA-I mimetic peptide is a significant advance in the oral delivery of peptides as therapies for cardiovascular disease and other chronic inflammatory disorders.

Summary In the past year, there have been important advances in the field of apoA-I mimetic peptides, including the oral delivery of bioactive peptides. Further work is required to fully understand the molecular basis for the effect of the peptide on the intestine and bioactive oxidized lipids.

The University of Chicago, Department of Pathology, Chicago, Illinois, USA

Correspondence to Godfrey S. Getz, University of Chicago, Box MC 1089, 5841 S. Maryland Avenue, Chicago, IL 60637, USA. Tel: +1 773 834 4856; fax: +1 773 834 5251; e-mail: getz@bsd.uchicago.edu

© 2014 Wolters Kluwer Health | Lippincott Williams & Wilkins