Binding of glycoprotein β₂-GPI with oxidized low density lipoprotein.

He Zhang; Jingda LI; Amei Chen; Qingping Liu

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Binding of glycoprotein β₂-GPI with oxidized low density lipoprotein.

Author: He ZHANG ¹ ; Jingda LI ¹ ; Amei CHEN ² ; Qingping LIU ¹
Author Information

1. Key Laboratory of the Glucolipid Metabolism, College of Life Science and Technology, Dalian University, Dalian 116000, Liaoning, China.
2. Department of Histology and Embryology, Inner Mongolia Medical University, Hohhot 010000, Inner Mongolia, China.
Publication Type:Journal Article
Keywords: 7-ketocholesteryl-9-carboxynonanoate ligand; binding mechanism; oxidized low density lipoprotein; recombinant fifth domain of β₂-glycoprotein I; β₂-glycoprotein I
From: Chinese Journal of Biotechnology 2017;33(1):122-131
CountryChina
Language:Chinese
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.