An apoA-I mimetic peptide containing a proline residue has greater in vivo HDL binding and anti-inflammatory ability than the 4F peptide
Open Access
- 1 September 2009
- journal article
- research article
- Published by Elsevier in Journal of Lipid Research
- Vol. 50 (9), 1889-1900
- https://doi.org/10.1194/jlr.m900151-jlr200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Anti-inflammatory apoA-I-mimetic peptides bind oxidized lipids with much higher affinity than human apoA-IJournal of Lipid Research, 2008
- Apolipoprotein A-I mimetic peptide helix number and helix linker influence potentially anti-atherogenic propertiesJournal of Lipid Research, 2008
- Lipoprotein inflammatory properties and serum amyloid A levels but not cholesterol levels predict lesion area in cholesterol-fed rabbitsJournal of Lipid Research, 2007
- Apolipoprotein A-I Mimetic PeptidesArteriosclerosis, Thrombosis, and Vascular Biology, 2005
- Mining biomarkers in human sera using proteomic toolsProteomics, 2004
- Metabolism of ApoA-I as Lipid-Free Protein or as Component of Discoidal and Spherical Reconstituted HDLsArteriosclerosis, Thrombosis, and Vascular Biology, 2002
- Turnover of synthetic class A amphipathic peptide analogues of exchangeable apolipoproteins in rats. Correlation with physical properties.Arteriosclerosis and Thrombosis: A Journal of Vascular Biology, 1992
- Conformational studies on peptides with proline in the right‐handed α‐helical regionBiopolymers, 1990
- Helix geometry in proteinsJournal of Molecular Biology, 1988
- Renal filtration, transport, and metabolism of low-molecular-weight proteins: A reviewKidney International, 1979