Abstract

Apolipoprotein A-I (apoA-I) is a major protein constituent of high density lipoprotein (HDL) which plays a prominent role in reverse cholesterol transport as well as other functions of HDL. Oxidative stress in many inflammatory conditions leads to peroxidation of phospholipids resulting in the formation of oxidized HDL particles. Effect of oxidized phospholipids on the properties of HDL is not well characterized. In this study we have characterized the effect of oxidized phospholipids on the properties of reconstituted HDL particles. Reconstituted HDL particles containing varying amount of oxidized-PAPC were prepared by cholate dialysis method and purified using gel filtration chromatography. Purified rHDL particles were used for characterization. Our results indicate that presence of oxidized-PAPC not only modifies the lipidic environment of HDL particles but also drastically alters the secondary structure and stability of bound apoA-I and induces significant change in global conformation as well as orientation of bound apoA-I. We acknowledge financial support from NIPER, S.A.S. Nagar, India.

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