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• W4310673855 abstract "Staphylococcal protein A (SpA) domain B (the basis of affibody) has been widely used in affinity chromatography and found therapeutic applications against inflammatory diseases through targeting the Fc part of immunoglobulin G (IgG). We have performed extensive molecular dynamics simulation of 41 SpA mutants and compared their dynamics and conformations to wild type. The simulations revealed the molecular details of structural and dynamics changes that occurred due to introducing point mutations and helped to explain the SPR results. It was observed in some variants a point mutation caused extensive structural changes far from the mutation site, while an effect of some other mutations was limited to the site of the mutated residue. Also, the pattern of hydrogen bond networks and hydrophobic core arrangements were investigated. We figured out mutations that occurred at positions 128, 136, 150 and 153, affected two hydrophobic cores at the interface as well as mutations introduced at positions 129 and 154 interrupted two hydrogen bond networks of the interface, SPR data showed all of these mutations reduced binding affinity significantly. Overall, by scanning the SpA-Fc interface through the large numbers of introduced mutations, the new insights have been gained which would help to design high- affinity ligands of IgG." @default.
• W4310673855 created "2022-12-15" @default.
• W4310673855 creator A5035139420 @default.
• W4310673855 creator A5088774091 @default.
• W4310673855 date "2023-03-01" @default.
• W4310673855 modified "2023-09-30" @default.
• W4310673855 title "New insights into the effect of mutations on affibody-Fc interaction, a molecular dynamics simulation approach" @default.
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• W4310673855 doi "https://doi.org/10.1016/j.jsb.2022.107925" @default.
• W4310673855 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36470559" @default.
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