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• W2025879873 abstract "The high affinity and specificity between avidin and biotin were employed to bind a recombinant single-chain antibody fragment to synthetic hydrophilic polymer drug carriers. Two semitelechelic polymers, based on poly(ethylene glycol) and poly[ N-(2-hydroxypropyl)methacrylamide], each containing a single thiol end group, were conjugated to dithiopyridyl-modified avidin. The biotinylated recombinant single-chain antibody fragment of the M75 antibody was then noncovalently bound to the polymer-avidin conjugates. The recombinant protein was chosen as a targeting ligand against carbonic anhydrase IX, a marker overexpressed by tumor cells of various human carcinomas. The antigen-binding affinity of the polymer–single-chain antibody fragment complex was confirmed by enzyme-linked immuno sorbent assay (ELISA). This approach provides an original, nondestructive way of preparing supramolecular systems intended for targeted delivery of therapeutics utilizing modern chemical procedures, including reversible addition–fragmentation chain-transfer polymerization and recombinant DNA techniques." @default.
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• W2025879873 date "2013-05-01" @default.
• W2025879873 modified "2023-10-02" @default.
• W2025879873 title "Avidin-conjugated polymers with monobiotinylated antibody fragments: A new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics" @default.
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• W2025879873 doi "https://doi.org/10.1177/0883911513486225" @default.
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