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제125회 대한화학회 학술발표회 및 총회 Solvation Free Energy Change in Monoclonal Antibodies by Point Mutations

2020년 2월 3일 14시 08분 54초
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Physical Chemistry
저자 및
Jihyeon Lee, Song-Ho Chong, Sihyun Ham*
Department of Chemistry, Sookmyung Women's University, Korea
Monoclonal antibody (mAb) has been developed for immune and inflammatory diseases as well as cancer. Although it exhibits an aggregation propensity in high concentrations which are required to be injected to treat the diseases, decreasing the solvation free energy can improve it. In this study, we report all-atom, explicit-water molecular dynamics simulations of two publicly known IgG1 monoclonal antibodies, mAb1 and mAb2, and the computation of the free energy with three-dimensional reference interaction site model theory. We find that the interactions among residues near the mutation sites have an effects on solubility of the proteins. The difference in solvation free energy of mAbs is decreased as their residues are hindered forming salt bridges and hydrogen bonds by point mutation. In addition, we observe that the mutants get unfavorable solvation free energies depending on the local surface charges around the mutation site on mAbs compared to the respective wild-types. These results may help inform future studies of engineering of monoclonal antibodies as biotherapeutics.