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

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.

journal_name

Chem Phys Lipids

authors

White CR,Datta G,Wilson L,Palgunachari MN,Anantharamaiah GM

doi

10.1016/j.chemphyslip.2019.01.009

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

28-35

eissn

0009-3084

issn

1873-2941

pii

S0009-3084(18)30185-3

journal_volume

219

pub_type

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