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Biocompatible Size‐Defined Dendrimer–Albumin Binding Protein Hybrid Materials as a Versatile Platform for Biomedical Applications
Author(s) -
Maly Jan,
Stanek Ondrej,
Frolik Jan,
Maly Marek,
Ennen Franka,
Appelhans Dietmar,
Semeradtova Alena,
Wrobel Dominika,
Stofik Marcel,
Knapova Tereza,
Kuchar Milan,
Stastna Lucie Cervenkova,
Cermak Jan,
Sebo Peter,
Maly Petr
Publication year - 2016
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201500332
Subject(s) - dendrimer , chemistry , streptavidin , human serum albumin , biotinylation , combinatorial chemistry , scaffold , conjugate , drug delivery , covalent bond , biophysics , nanotechnology , polymer chemistry , organic chemistry , biochemistry , materials science , biotin , biomedical engineering , medicine , mathematical analysis , mathematics , biology
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.