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A more recent version of this article appeared on September 1, 2007

Papers In Press, published online ahead of print June 14, 2007
J. Lipid Res., doi:10.1194/jlr.R700010-JLR200
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Submitted on May 3, 2007
Revised on June 12, 2007
Accepted on June 13, 2007

Structural requirements for anti-oxidative and anti-inflammatory properties of apo A-I mimetic peptides

G. M. Anantharamaiah, Vinod K. Mishra, David W. Garber, Geeta Datta, Shaila P. Handattu, Mayakonda N. Palgunachari, Manjula Chaddha, Mohamad Navab, Srinivas T. Reddy, Jere P. Segrest, and Alan M. Fogelman

Medicine, University of Alabama at Birmingham, Birmingham, AL 35294

Corresponding Author: Ananth{at}uab.edu

Recently, attention has been focused on pharmacological treatments that elevate HDL cholesterol in order to prevent coronary artery disease. Despite three decades of extensive research of human apolipoprotein (apo) A-I, the major protein component of HDL, the molecular basis for its antiatherogenic and anti-inflammatory functions remain elusive. Another protein component of HDL, apo A-II, has structural features similar to those of apo A-I but does not possess atheroprotective properties. To understand the molecular basis for the effectiveness of apo A-I, we used model synthetic peptides. We designed analogs of the class A amphipathic helical motif in apo A-I which is responsible for solubilizing phospholipids. None of these analogs has sequence homology to apo A-I but all are similar in their lipid-associating structural motif. Although all of these peptide analogs interact with phospholipids to form peptide:lipid complexes, the biological properties of these analogs are different. Physical-chemical and NMR studies of these peptides have enabled the delineation of structural requirements for atheroprotective and anti-inflammatory properties in these peptides. It has been shown that peptides that interact strongly with lipid acyl chains do not have anti-atherogenic and anti-inflammatory properties. In contrast, peptides that associate close to the lipid head group (and hence do not interact strongly with the lipid acyl chain) are anti-atherogenic and anti-inflammatory. Understanding the structure and function of apo A-I and HDL through studies of the amphipathic helix motif may lead to peptide-based therapies for inhibiting atherosclerosis and other related inflammatory lipid disorders.


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