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Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity

Single-chain antibody mutants have been evolved in vitro with antigen-binding equilibrium dissociation constant K(d) = 48 fM and slower dissociation kinetics (half-time > 5 days) than those for the streptavidin–biotin complex. These mutants possess the highest monovalent ligand-binding affinity yet...

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Publicado en:Proc Natl Acad Sci U S A
Autores principales: Boder, Eric T., Midelfort, Katarina S., Wittrup, K. Dane
Formato: Artigo
Lenguaje:Inglês
Publicado: National Academy of Sciences 2000
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Acceso en línea:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC27086/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10984501/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.170297297
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