Abstract
Levels of high density lipoprotein (HDL) and its major protein component, apolipoprotein (apo) A-I, are strongly inversely correlated to risk of atherosclerosis and other vascular diseases. A number of properties of apo A-I may contribute to this protection, including removal of cholesterol from peripheral tissues to the liver (reverse cholesterol transport), anti-inflammatory and anti-oxidative activities, and modulation of vascular function. Apo A-I has lipidassociating domains that form class A amphipathic helices. Peptide analogs that have no sequence homology to the domains in apo A-I but possess the class A motif have been shown to not only associate with phospholipid but also mimic several of the functional properties of apo A-I. Peptide 4F, with four phenylalanines on the non-polar face, was found to be maximally effective in mimicking the positive qualities of apo A-I; this peptide inhibited atherosclerosis, reduced inflammation and oxidation, and improved vascular function in a number of animal models, and when synthesized with Damino acids is orally bioavailable. Several other classes of peptide mimetics are now being studied, and may contribute to our understanding of the functions of apo E and apo J. The use of peptide mimetics to study apolipoprotein function has proved to be a powerful tool, and may lead to novel therapeutic agents in the prevention of atherosclerosis and other vascular diseases.
Keywords: LDL metabolism, Apo A-I, Reverse cholesterol transport (RCT), lipopolysaccharide binding protein (LBP), Apo J Peptides
Current Pharmaceutical Biotechnology
Title: Atherosclerosis and Vascular Disease: Effects of Peptide Mimetics of Apolipoproteins
Volume: 7 Issue: 4
Author(s): David W. Garber, Shaila P. Handattu, Geeta Datta, Vinod K. Mishra, Himanshu Gupta, C. Roger White and G. M. Anantharamaiah
Affiliation:
Keywords: LDL metabolism, Apo A-I, Reverse cholesterol transport (RCT), lipopolysaccharide binding protein (LBP), Apo J Peptides
Abstract: Levels of high density lipoprotein (HDL) and its major protein component, apolipoprotein (apo) A-I, are strongly inversely correlated to risk of atherosclerosis and other vascular diseases. A number of properties of apo A-I may contribute to this protection, including removal of cholesterol from peripheral tissues to the liver (reverse cholesterol transport), anti-inflammatory and anti-oxidative activities, and modulation of vascular function. Apo A-I has lipidassociating domains that form class A amphipathic helices. Peptide analogs that have no sequence homology to the domains in apo A-I but possess the class A motif have been shown to not only associate with phospholipid but also mimic several of the functional properties of apo A-I. Peptide 4F, with four phenylalanines on the non-polar face, was found to be maximally effective in mimicking the positive qualities of apo A-I; this peptide inhibited atherosclerosis, reduced inflammation and oxidation, and improved vascular function in a number of animal models, and when synthesized with Damino acids is orally bioavailable. Several other classes of peptide mimetics are now being studied, and may contribute to our understanding of the functions of apo E and apo J. The use of peptide mimetics to study apolipoprotein function has proved to be a powerful tool, and may lead to novel therapeutic agents in the prevention of atherosclerosis and other vascular diseases.
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Cite this article as:
Garber W. David, Handattu P. Shaila, Datta Geeta, Mishra K. Vinod, Gupta Himanshu, Roger White C. and Anantharamaiah M. G., Atherosclerosis and Vascular Disease: Effects of Peptide Mimetics of Apolipoproteins, Current Pharmaceutical Biotechnology 2006; 7 (4) . https://dx.doi.org/10.2174/138920106777950834
DOI https://dx.doi.org/10.2174/138920106777950834 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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