Avidin-conjugated polymers with monobiotinylated antibody fragments: a new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics

0393213 - ÚMCH 2014 RIV GB eng J - Článek v odborném periodiku
Laga, Richard - Pola, Robert - Ulbrich, Karel - Hořejší, Magdalena - Sieglová, Irena - Král, Vlastimil - Fábry, Milan - Pechar, Michal
Avidin-conjugated polymers with monobiotinylated antibody fragments: a new strategy for the noncovalent attachment of recombinant proteins for polymer therapeutics.
Journal of Bioactive and Compatible Polymers. Roč. 28, č. 3 (2013), s. 289-299. ISSN 0883-9115. E-ISSN 1530-8030
Grant CEP: GA ČR GCP207/12/J030; GA AV ČR IAAX00500803
Výzkumný záměr: CEZ:AV0Z50520514
Institucionální podpora: RVO:61389013 ; RVO:68378050
Klíčová slova: avidin-biotin complex * polymer therapeutics * drug targeting
Kód oboru RIV: CD - Makromolekulární chemie
Impakt faktor: 2.500, rok: 2013

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.
Trvalý link: http://hdl.handle.net/11104/0223796