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Biocompatible Size-Defined Dendrimer-Albumin Binding Protein Hybrid Materials as a Versatile Platform for Biomedical Applications
J. Maly, O. Stanek, J. Frolik, M. Maly, F. Ennen, D. Appelhans, A. Semeradtova, D. Wrobel, M. Stofik, T. Knapova, M. Kuchar, LC. Stastna, J. Cermak, P. Sebo, P. Maly,
Language English Country Germany
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
- MeSH
- Bacterial Proteins genetics metabolism MeSH
- Biotin chemistry MeSH
- Biotinylation MeSH
- Cell Line MeSH
- Dendrimers chemical synthesis pharmacology MeSH
- Epithelial Cells cytology drug effects MeSH
- Escherichia coli genetics metabolism MeSH
- Gene Expression MeSH
- Rats MeSH
- Drug Delivery Systems * MeSH
- Humans MeSH
- Ligands MeSH
- Models, Molecular MeSH
- Nanoparticles chemistry ultrastructure MeSH
- Polyamines chemistry MeSH
- Polyethylene Glycols chemistry MeSH
- Recombinant Fusion Proteins genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Serum Albumin chemistry MeSH
- Streptavidin chemistry MeSH
- Streptomyces genetics metabolism MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
For the design of a biohybrid structure as a ligand-tailored drug delivery system (DDS), it is highly sophisticated to fabricate a DDS based on smoothly controllable conjugation steps. This article reports on the synthesis and the characterization of biohybrid conjugates based on noncovalent conjugation between a multivalent biotinylated and PEGylated poly(amido amine) (PAMAM) dendrimer and a tetrameric streptavidin-small protein binding scaffold. This protein binding scaffold (SA-ABDwt) possesses nM affinity toward human serum albumin (HSA). Thus, well-defined biohybrid structures, finalized by binding of one or two HSA molecules, are available at each conjugation step in a controlled molar ratio. Overall, these biohybrid assemblies can be used for (i) a controlled modification of dendrimers with the HSA molecules to increase their blood-circulation half-life and passive accumulation in tumor; (ii) rendering dendrimers a specific affinity to various ligands based on mutated ABD domain, thus replacing tedious dendrimer-antibody covalent coupling and purification procedures.
Institute of Biotechnology CAS v v i Pru˚myslová 595 Vestec 252 42 Jesenice u Prahy Czech Republic
Institute of Chemical Process Fundamentals CAS v v i Rozvojová 135 165 02 Prague Czech Republic
Institute of Microbiology CAS v v i Vídeˇnská 1083 142 20 Prague Czech Republic
Leibniz Institute of Polymer Research Dresden Hohe Straße 6 D 01069 Dresden Germany
References provided by Crossref.org
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