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Papers In Press, published online ahead of print June 14, 2007
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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.
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
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