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Updated: Feb 22, 2026

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
[Binding of glycoprotein β₂-GPI with oxidized low density lipoprotein]
He Zhang1, Jingda Li1, Amei Chen2
1Key Laboratory of the Glucolipid Metabolism, College of Life Science and Technology, Dalian University, Dalian 116000, Liaoning, China.
Abstract:
We analyzed the binding of P.rβ₂-GPI-DV with ox-LDL by fluorescence, molecular simulation and circular dichroism. We used SDS-PAGE and Western blotting to identify the purity of P.rβ₂-GPI-DV, fluorescence, circular dichroism spectroscopy and molecular docking simulation to analyze the binding between P.rβ₂-GPI-DV and oxLDL. P.rβ₂-GPI-DV was specifically recognized by anti-His antibody at 12 kDa position. The chromophoric groups, the changes of secondary structure and the molecular docking simulations revealed that the active pocket formed by Cys281-Lys-Asn-Lys-Glu-Lys-Lys287 and Leu313-Ala-Phe-Trp316 of P.rβ₂-GPI-DV and the -COOH carboxyl of oxLig-1 were the key for binding. P.rβ₂-GPI combined with ox-LDL via the fifth functional domain and the -COOH group. Our findings provide theoretical basis to further study the binding between β₂-GPI and ox-LDL in serum.
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