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• W4384493054 abstract "Phage display and biopanning are powerful tools for generating binding molecules for a specific target. However, the selection process based only on binding affinity provides no assurance for the antibody's affinity to the target epitope. In this study, we propose a molecular-evolution approach guided by native protein-protein interactions to generate epitope-targeting antibodies. The binding-site sequence in a native protein was grafted into a complementarity-determining region (CDR) in the nanobody, and a nonrelated CDR loop (in the grafted nanobody) was randomized to create a phage display library. In this construction of nanobodies by integrating graft and evolution technology (CAnIGET method), suitable grafting of the functional sequence added functionality to the nanobody, and the molecular-evolution approach enhanced the binding function to inhibit the native protein-protein interactions. To apply for biological tool with growth screening, model nanobodies with an affinity for filamenting temperature-sensitive mutant Z (FtsZ) from Staphylococcus aureus were constructed and completely inhibited the polymerization of FtsZ as a function. Consequently, the expression of these nanobodies drastically decreased the cell division rate. We demonstrate the potential of the CAnIGET method with the use of native protein-protein interactions for steady epitope-specific evolutionary engineering." @default.
• W4384493054 created "2023-07-18" @default.
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• W4384493054 date "2023-07-26" @default.
• W4384493054 modified "2023-10-17" @default.
• W4384493054 title "Synthesis of epitope‐targeting nanobody based on native protein–protein interactions for FtsZ filamentation suppressor" @default.
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• W4384493054 doi "https://doi.org/10.1002/biot.202300039" @default.
• W4384493054 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37458140" @default.
• W4384493054 hasPublicationYear "2023" @default.
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