期刊
TRENDS IN BIOTECHNOLOGY
卷 31, 期 11, 页码 612-620出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2013.07.002
关键词
monoclonal antibody; IgG; V-H; V-L; scFv; Fv; Fab; variable domain; complementarity-determining region (CDR); bispecific; solubility; antibody engineering
资金
- National Science Foundation (CBET grants) [0954450, 1159943]
- Pew Charitable Trust (Pew Scholars Award in Biomedical Sciences)
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1159943, 0954450] Funding Source: National Science Foundation
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.
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