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The apoA-I mimetic peptide 4F protects apolipoprotein A-I from oxidative damage.
- Source :
-
Chemistry & Physics of Lipids . Mar2019, Vol. 219, p28-35. 8p. - Publication Year :
- 2019
-
Abstract
- Highlights • New nanoparticles using human apoA-I and well-characterized apoA-I mimetic peptide 4F with POPC in the absence of chemical detergents. • Presence of 4F in nanoparticles potentially enhances biological activities of human apoAI:lipid nanoparticles. • New nanoparticles are stable to oxidative process. • ApoA-I-4F:POPC nanoparticles potentially ameliorate lipid-mediated disorders more effectively than apoA-I:POPC nanodiscs. Abstract High density lipoprotein (HDL) is prone to modification by the oxidizing and chlorinating agent hypochlorite anion (OCl−). Oxidation of apolipoprotein (apo) A-I, the major protein in HDL, reduces ABCA-1 mediated cholesterol efflux and other protective responses to HDL. The apoA-I mimetic peptide 4F has been shown to undergo oxidation; however, the ability of the peptide to mediate cholesterol efflux remains intact. Here, we show that 4F protects apoA-I from hypochlorite-mediated oxidation. Mass spectral analysis of apoA-I shows that tyrosine residues that are prone to hypochlorite-mediated chlorination are protected in the presence of 4F. Furthermore, 4F enhances the cholesterol efflux ability of apoA-I to a greater extent than either 4F or apoA-I alone, even after hypochlorite oxidation. These observations suggest that apoA-I in lipid complexes may be protected by the presence of 4F, resulting in the preservation of its anti-inflammatory and anti-atherogenic properties. These studies also form the basis for the future studies of nanoparticles possessing both apoA-I and 4F. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00093084
- Volume :
- 219
- Database :
- Academic Search Index
- Journal :
- Chemistry & Physics of Lipids
- Publication Type :
- Academic Journal
- Accession number :
- 134863599
- Full Text :
- https://doi.org/10.1016/j.chemphyslip.2019.01.009