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• W2034006833 abstract "•Therapeutic antibodies possess highly variable propensities to aggregate. •Antibody CDRs, frameworks, and domain interfaces strongly influence solubility. •Computational methods are emerging for designing aggregation-resistant antibodies. •These predictive methods are yielding antibodies with high solubility and affinity. Monoclonal antibodies are attractive therapeutics for treating a wide range of human disorders due to their exquisite binding specificity and high binding affinity. However, a limitation of antibodies is their highly variable and difficult-to-predict propensities to aggregate when concentrated during purification and delivery. Despite the large size and complex structure of antibodies, recent findings suggest that antibody solubility can be dramatically improved using rational design methods in addition to conventional selection methods. Here, we review key advances and unmet challenges in engineering the variable and constant regions of antibody fragments and full-length antibodies to resist aggregation without reducing their binding affinity. These experimental and computational discoveries should accelerate the development of robust algorithms for designing aggregation-resistant antibodies. Monoclonal antibodies are attractive therapeutics for treating a wide range of human disorders due to their exquisite binding specificity and high binding affinity. However, a limitation of antibodies is their highly variable and difficult-to-predict propensities to aggregate when concentrated during purification and delivery. Despite the large size and complex structure of antibodies, recent findings suggest that antibody solubility can be dramatically improved using rational design methods in addition to conventional selection methods. Here, we review key advances and unmet challenges in engineering the variable and constant regions of antibody fragments and full-length antibodies to resist aggregation without reducing their binding affinity. These experimental and computational discoveries should accelerate the development of robust algorithms for designing aggregation-resistant antibodies. antibody fragment containing the VH, CH1, VL and CL domains first constant domain of the heavy chain adjacent to the VH domain constant domain of the light chain peptide loop in the VH or VL domains that is involved in binding to antigens domain antibody fragment such as single VH or VL domains Grafted AMyloid-Motif AntiBODY that binds to amyloid fibrils and related conformers crystallizable domain containing two CH2 and two CH3 domains monoclonal antibody antibody fragment composed of VH and VL domains connected via a peptide linker a measure of the dynamic exposure of hydrophobic patches on protein surfaces an approach to solubilizing proteins in which many solvent-exposed residues are mutated to charged residues of the same polarity variable domain of the heavy chain variable domain of the light chain" @default.
• W2034006833 created "2016-06-24" @default.
• W2034006833 creator A5025704650 @default.
• W2034006833 creator A5029310606 @default.
• W2034006833 creator A5041041267 @default.
• W2034006833 date "2013-11-01" @default.
• W2034006833 modified "2023-10-14" @default.
• W2034006833 title "Toward aggregation-resistant antibodies by design" @default.
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• W2034006833 doi "https://doi.org/10.1016/j.tibtech.2013.07.002" @default.
• W2034006833 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23932102" @default.
• W2034006833 hasPublicationYear "2013" @default.
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