Format

Send to

Choose Destination
Chem Phys Lipids. 2019 Mar;219:28-35. doi: 10.1016/j.chemphyslip.2019.01.009. Epub 2019 Jan 29.

The apoA-I mimetic peptide 4F protects apolipoprotein A-I from oxidative damage.

Author information

1
Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, United States.
2
Targeted Metabolomics and Proteomics Laboratory, University of Alabama at Birmingham, Birmingham, AL, 35294, United States.
3
Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, United States; Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL, 35294, United States. Electronic address: Ananth@uab.edu.

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.

KEYWORDS:

ApoA-I; ApoA-I mimetic peptide; Cholesterol efflux; Hypochlorous acid; Oxidation

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center