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Hyperproduction of immunoglobulin G (IgG) is a major pathogenic factor in autoimmune diseases. Specific sorbents are used to eliminate the high level of IgG. Molecular docking can be used as a tool for theoretical search for sorbent ligands for the IgG removal from biological fluids. Using docking, modeling of amino acid interactions with IgG ligands was performed. Based on the docking results, active amino acids were identified and possible combinations of them were proposed for the creation of diand tripeptide sequences. As a result, aromatic amino acids (Tyr, Trp, Phe), di-and tripeptides based on them (Trp-DTyr, Phe-DTyr, Trp-Phe-DTyr, Phe-Trp-DTyr) were found to have high activity for IgG proteins, and three peptides (Trp-Phe-DTyr, Phe-Trp-DTyr) not only show high activity to total IgG, but can also be divided in their activity relative to subclasses of class G immunoglobulins.