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Updated: Jun 3, 2026
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Molecular mechanism of the affinity interactions between protein A and human immunoglobulin G1 revealed by molecular
Bo Huang1, Fu-Feng Liu, Xiao-Yan Dong
1Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
Abstract:
Protein A (SpA) affinity chromatography has been widely used for the purification of immunoglobulin G (IgG). However, the molecular mechanism of the affinity between IgG and SpA remains unclear. In this work, molecular dynamics simulations and molecular mechanics-Poisson-Boltzmann surface area analysis were performed to investigate the molecular mechanism of the affinity interactions. It is found that hydrophobic interaction contributes more than 80% to the binding free energy, while electrostatic interaction plays a minor role (<20%). Through free energy decomposition and pair interaction analysis, the hot spots of the SpA-hIgG1 complex are identified. For hIgG1, the hot spots include the residues of I253, H310, Q311, D315, K317, E430, and N434. For SpA, residues F132, Y133, H137, E143, R146, and K154 contribute significantly. Furthermore, helix I of SpA binds Fc through hydrophobic interaction, while helix II mainly provides electrostatic interaction that determines the binding selectivity to different Igs. Finally, the binding motif of SpA is constructed, which would help design novel high-affinity ligands of IgG.
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