iBodies: Modular Synthetic Antibody Mimetics Based on Hydrophilic Polymers Decorated with Functional Moieties
Autor: | Vladimir Subr, Tomáš Knedlík, Pavel Šácha, Karel Ulbrich, Václav Navrátil, Frantisek Sedlak, Jan Tykvart, Jiří Schimer, Jan Konvalinka, Jiří Strohalm, Pavel Majer, Petra Dvořáková, Jan Parolek |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Polymers Immunoprecipitation 010402 general chemistry medicine.disease_cause 01 natural sciences Antibodies Catalysis 03 medical and health sciences Molecular recognition Antibody Mimetics Cell Line Tumor HPMA Protein purification Protein targeting protein targeting medicine Humans polymer conjugates Chemistry Ligand Communication Molecular Mimicry Chemical modification General Medicine General Chemistry Combinatorial chemistry Communications 0104 chemical sciences Synthetic antibody 030104 developmental biology molecular recognition Hydrophobic and Hydrophilic Interactions Conjugate |
Zdroj: | Angewandte Chemie (International Ed. in English) |
ISSN: | 1433-7851 |
Popis: | Antibodies are indispensable tools for biomedicine and anticancer therapy. Nevertheless, their use is compromised by high production costs, limited stability, and difficulty of chemical modification. The design and preparation of synthetic polymer conjugates capable of replacing antibodies in biomedical applications such as ELISA, flow cytometry, immunocytochemistry, and immunoprecipitation is reported. The conjugates, named “iBodies”, consist of an HPMA copolymer decorated with low‐molecular‐weight compounds that function as targeting ligands, affinity anchors, and imaging probes. We prepared specific conjugates targeting several proteins with known ligands and used these iBodies for enzyme inhibition, protein isolation, immobilization, quantification, and live‐cell imaging. Our data indicate that this highly modular and versatile polymer system can be used to produce inexpensive and stable antibody substitutes directed toward virtually any protein of interest with a known ligand. |
Databáze: | OpenAIRE |
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