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Authors Maly, J. ; Stanek, O. ; Frolik, J. ; Maly, M. ; Ennen, F. ; Appelhans, D. ; Semeradtova, A. ; Wrobel, D. ; Stofik, M. ; Knapova, T. ; Kuchar, M. ; Cervenkova-Stastna, L. ; Cermak, J. ; Sebo, P. ; Maly, P.
Title Biocompatible size-defined dendrimer-albumin binding protein hybrid materials as a versatile platform for biomedical applications
Date 01.04.2016
Number 49287
Abstract 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.
Publisher Macromolecular Bioscience
Wikidata
Citation Macromolecular Bioscience 16 (2016) 553-566
DOI https://doi.org/10.1002/mabi.201500332
Tags binding domain proteins biohybrid structures hsa pamam dendrimer streptavidin-biotin conjugations

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