Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developability.

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作者： James T,Heads ^[1] ; Richard,Lamb ^[1] ; Sebastian,Kelm ^[1] ; Ralph,Adams ^[1] ; Peter,Elliott ^[1] ; Kerry,Tyson ^[1] ; Sarfaraj,Topia ^[1] ; Shauna,West ^[1] ; Ruodan,Nan ^[1] ; Alison,Turner ^[1] ; Alastair D G,Lawson ^[1]

作者单位： UCB Pharma, Slough, Berkshire SL1 3WE, UK. ^[1]

关键词 Fab Fv IgG1 IgG4P aggregation antibody isotype mAb prediction

主题词氨基酸取代(Amino Acid Substitution);免疫球蛋白G(Immunoglobulin G);模型, 分子(Models, Molecular);蛋白质构象(Protein Conformation);蛋白质工程(Protein Engineering);静电(Static Electricity)

DOI 10.1093/protein/gzz046

PMID 31868219

发布时间 2020-07-14

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Protein engineering, design & selection

2019年32卷6期

277-288页

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Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developability.

Protein engineering, design & selection

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Protein engineering, design & selection

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Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developability.

Protein engineering, design & selection

相似文献

Protein engineering, design & selection

相关期刊

检索历史清除