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Biocompatible Size-Defined Dendrimer-Albumin Binding Protein Hybrid Materials as a Versatile Platform for Biomedical Applications

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    SYSNO ASEP0462486
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleBiocompatible Size-Defined Dendrimer-Albumin Binding Protein Hybrid Materials as a Versatile Platform for Biomedical Applications
    Author(s) Malý, J. (CZ)
    Staněk, Ondřej (MBU-M) RID, ORCID
    Frolík, J. (CZ)
    Malý, M. (CZ)
    Ennen, F. (DE)
    Appelhans, D. (DE)
    Semerádtová, A. (CZ)
    Wróbel, D. (CZ)
    Stofik, M. (CZ)
    Knapová, T. (CZ)
    Kuchař, Milan (BTO-N) RID
    Červenková Šťastná, Lucie (UCHP-M) RID, ORCID, SAI
    Čermák, Jan (UCHP-M) RID, ORCID, SAI
    Šebo, Peter (MBU-M) RID, ORCID
    Malý, Petr (BTO-N) RID, ORCID
    Source TitleMacromolecular Bioscience. - : Wiley - ISSN 1616-5187
    Roč. 16, č. 4 (2016), s. 553-566
    Number of pages14 s.
    Languageeng - English
    CountryDE - Germany
    Keywordsbinding domain proteins ; biohybrid structures ; HSA
    Subject RIVCE - Biochemistry
    Subject RIV - cooperationInstitute of Biotechnology - Genetics ; Molecular Biology
    R&D ProjectsGA15-05903S GA ČR - Czech Science Foundation (CSF)
    QJ1210041 GA MZe - Ministry of Agriculture (MZe)
    ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Institutional supportMBU-M - RVO:61388971 ; BTO-N - RVO:86652036 ; UCHP-M - RVO:67985858
    UT WOS000374262100008
    EID SCOPUS84970897350
    DOI10.1002/mabi.201500332
    AnnotationFor 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.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2017
Number of the records: 1  

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