Biocompatible Size-Defined Dendrimer-Albumin Binding Protein Hybrid Materials as a Versatile Platform for Biomedical Applications
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Grant support
P41-GM103311
NIGMS NIH HHS - United States
- Keywords
- HSA, PAMAM dendrimer, Streptavidin-biotin conjugations, binding domain proteins, biohybrid structures,
- 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
- Names of Substances
- Bacterial Proteins MeSH
- Biotin MeSH
- Dendrimers MeSH
- Ligands MeSH
- PAMAM Starburst MeSH Browser
- Polyamines MeSH
- Polyethylene Glycols MeSH
- Recombinant Fusion Proteins MeSH
- Serum Albumin MeSH
- Streptavidin 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
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