Avidin-conjugated polymers with monobiotinylated antibody fragments: A new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics
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 si...
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Veröffentlicht in: | Journal of bioactive and compatible polymers 2013-05, Vol.28 (3), p.289-299 |
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container_title | Journal of bioactive and compatible polymers |
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creator | Laga, Richard Pola, Robert Ulbrich, Karel Horřejší, Magda Sieglová, Irena Král, Vlastimil Fábry, Milan Pechar, Michal |
description | 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. |
doi_str_mv | 10.1177/0883911513486225 |
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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). 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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.</description><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Chemical modifications</subject><subject>Chemical reactions and properties</subject><subject>Exact sciences and technology</subject><subject>General pharmacology</subject><subject>Medical sciences</subject><subject>Organic polymers</subject><subject>Pharmaceutical technology. Pharmaceutical industry</subject><subject>Pharmacology. 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Pharmaceutical industry</topic><topic>Pharmacology. Drug treatments</topic><topic>Physicochemistry of polymers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Laga, Richard</creatorcontrib><creatorcontrib>Pola, Robert</creatorcontrib><creatorcontrib>Ulbrich, Karel</creatorcontrib><creatorcontrib>Horřejší, Magda</creatorcontrib><creatorcontrib>Sieglová, Irena</creatorcontrib><creatorcontrib>Král, Vlastimil</creatorcontrib><creatorcontrib>Fábry, Milan</creatorcontrib><creatorcontrib>Pechar, Michal</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of bioactive and compatible polymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Laga, Richard</au><au>Pola, Robert</au><au>Ulbrich, Karel</au><au>Horřejší, Magda</au><au>Sieglová, Irena</au><au>Král, Vlastimil</au><au>Fábry, Milan</au><au>Pechar, Michal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Avidin-conjugated polymers with monobiotinylated antibody fragments: A new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics</atitle><jtitle>Journal of bioactive and compatible polymers</jtitle><date>2013-05-01</date><risdate>2013</risdate><volume>28</volume><issue>3</issue><spage>289</spage><epage>299</epage><pages>289-299</pages><issn>0883-9115</issn><eissn>1530-8030</eissn><coden>JBCPEV</coden><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.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><doi>10.1177/0883911513486225</doi><tpages>11</tpages></addata></record> |
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subjects | Applied sciences Biological and medical sciences Chemical modifications Chemical reactions and properties Exact sciences and technology General pharmacology Medical sciences Organic polymers Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Physicochemistry of polymers |
title | Avidin-conjugated polymers with monobiotinylated antibody fragments: A new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics |
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