J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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Originally published In Press as doi:10.1194/jlr.R700010-JLR200 on June 14, 2007

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Journal of Lipid Research, Vol. 48, 1915-1923, September 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Review

Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides

G. M. Anantharamaiah1,*, Vinod K. Mishra*, David W. Garber*, Geeta Datta*, Shaila P. Handattu*, Mayakonda N. Palgunachari*, Manjula Chaddha*, Mohamad Navab{dagger}, Srinivasa T. Reddy{dagger}, Jere P. Segrest* and Alan M. Fogelman{dagger}

* Department of Medicine, Biochemistry, and Molecular Genetics and Atherosclerosis Research Unit, University of Alabama at Birmingham, Birmingham, AL 35294
{dagger} Department of Medicine, David Geffen School of Medicine at the University of California, Los Angeles, CA 90095-1679

Published, JLR Papers in Press, June 14, 2007.

1 To whom correspondence should be addressed. e-mail: ananth{at}uab.edu

Recently, attention has been focused on pharmacological treatments that increase HDL cholesterol to prevent coronary artery disease. Despite three decades of extensive research of human apolipoprotein A-I (apoA-I), the major protein component of HDL, the molecular basis for its antiatherogenic and anti-inflammatory functions remain elusive. Another protein component of HDL, apoA-II, has structural features similar to those of apoA-I but does not possess atheroprotective properties. To understand the molecular basis for the effectiveness of apoA-I, we used model synthetic peptides. We designed analogs of the class A amphipathic helical motif in apoA-I that is responsible for solubilizing phospholipids. None of these analogs has sequence homology to apoA-I, but all are similar in their lipid-associating structural motifs. 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 antiatherogenic 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 antiatherogenic and anti-inflammatory. Understanding the structure and function of apoA-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.

Supplementary key words atherosclerosis • high density lipoprotein • hyperlipidemia • lipoproteins


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