Open AccessConstruction of immunoglobulin-binding peptides based on analysis of the protein A of <i>Staphylococcus aureus</i> interaction with immunoglobulins Fc fragment
Author(s) -
А. В. Лапко,
Е. С. Пустюльга,
В. П. Голубович
Publication year - 2019
Publication title -
vescì nacyânalʹnaj akadèmìì navuk belarusì. seryâ hìmìčnyh navuk
Language(s) - English
Resource type - Journals
eISSN - 2524-2342
pISSN - 1561-8331
DOI - 10.29235/1561-8331-2019-55-4-447-454
Subject(s) - staphylococcus aureus , docking (animal) , antibody , protein a , chemistry , fragment crystallizable region , amino acid , peptide , binding site , biochemistry , computational biology , peptide sequence , combinatorial chemistry , biology , bacteria , receptor , immunology , medicine , genetics , nursing , gene
Over the past decades, molecular docking has become an increasingly popular tool for the development of new drugs. To search and design new compounds, a detailed study of the interaction of existing complexes of ligands with the target protein is necessary. According to the purpose to identify amino acid residues of the B domain of protein A of Staphylococcus aureus involved in interaction with immunoglobulins G, we studied the interaction mechanisms during the formation of a complex of protein A of the Staphylococcus aureus cell wall and immunoglobulins G by molecular docking. By the means of molecular docking we selected four amino acid residues of Phe132, Gln129, Tyr133 and Phe124, which we can use to construct a peptide analog of the active binding site of protein A with the Fc fragment of immunoglobulins G. The obtained results can serve as starting point for an effective strategy for finding new medicines, in particular, they can be used to further develop biospecific sorbent for the selective removal of immunoglobulins G from human blood.