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The increasing importance of immunoglobulin (Ig) as therapeutics has led to the need for more efficient,robust,and lower cost production processes,and purification is the crucial step of the whole production process.Afiinity chromatography using protein A from Staphylococcus aureus (SPA) as a ligand has been widely used for the purification of IgG,but the molecular mechanism of the affimity between IgG and SpA remains unclear [1].In this work,molecular dynamics simulations and molecular mechanics-Poisson-Boltzmann surface area (MM/PBSA) [2] analysis are performed to investigate the affmity interactions of SpA-hIgGl complex.