Synthesis of Maleimide-Functionalyzed HPMA-Copolymers and in vitro Characterization of the aRAGE- and Human Immunoglobulin (huIgG)-Polymer Conjugates

Herein the synthesis of antibody–polymer conjugates, with a quite narrow dispersity based on the polymer HPMA, are reported. These conjugates are synthesized by coupling antibodies to maleimide‐functionalized poly(N‐(2‐hydroxypropyl)‐methacrylamide) (poly‐HPMA) copolymers derived through reversible...

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Veröffentlicht in:Macromolecular bioscience 2013-02, Vol.13 (2), p.203-214
Hauptverfasser: Tappertzhofen, Kristof, Metz, Verena V., Hubo, Mario, Barz, Matthias, Postina, Rolf, Jonuleit, Helmut, Zentel, Rudolf
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Sprache:eng
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Zusammenfassung:Herein the synthesis of antibody–polymer conjugates, with a quite narrow dispersity based on the polymer HPMA, are reported. These conjugates are synthesized by coupling antibodies to maleimide‐functionalized poly(N‐(2‐hydroxypropyl)‐methacrylamide) (poly‐HPMA) copolymers derived through reversible addition‐fragmentation chain transfer (RAFT) polymerization of pentafluorophenyl methacrylate via the intermediate step of an activated ester polymer. We develop a protocol that allows the attachment of two different model antibodies, monoclonal anti‐RAGE (receptor for advanced glycation end‐products) antibody, and polyclonal human immunoglobulin (huIgG). Modification of the antibody and conjugation is monitored by SDS‐PAGE electrophoresis. Preserved affinity is demonstrated by Western Blott and cell‐uptake analysis, for example, to cells of the immune system. The attachment of antibodies in an efficient binding protocol to biocompatible polymers is a promising tool to improve nanomedicines. Our route leads to conjugates with a narrow dispersity and retained binding activity, for example, to cells of the immune system.
ISSN:1616-5187
1616-5195
DOI:10.1002/mabi.201200344