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Raster image correlation spectroscopy as a novel tool to study interactions of macromolecules with nanofiber scaffolds

  1. 1.
    SYSNO ASEP0368065
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleRaster image correlation spectroscopy as a novel tool to study interactions of macromolecules with nanofiber scaffolds
    Author(s) Norris, S. C. P. (US)
    Humpolíčková, Jana (UFCH-W) RID
    Amler, Evžen (UEM-P) RID
    Huranová, Martina (UMG-J) ORCID
    Buzgo, Matej (UEM-P)
    Macháň, Radek (UFCH-W)
    Lukáš, D. (CZ)
    Hof, Martin (UFCH-W) RID, ORCID
    Source TitleActa Biomaterialia. - : Elsevier - ISSN 1742-7061
    Roč. 7, č. 12 (2011), s. 4195-4203
    Number of pages9 s.
    Languageeng - English
    CountryGB - United Kingdom
    Keywordsfluorecence dynamics ; transient binding ; diffusion
    Subject RIVCF - Physical ; Theoretical Chemistry
    R&D ProjectsLC06063 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    IAA500390702 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    GAP304/10/1307 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z40400503 - UFCH-W (2005-2011)
    AV0Z50390512 - UEM-P (2005-2011)
    AV0Z50390703 - UEM-P (2007-2013)
    AV0Z50520514 - UMG-J (2005-2011)
    UT WOS000297436500012
    DOI10.1016/j.actbio.2011.07.012
    AnnotationDynamic processes such as diffusion and binding/unbinding of macromolecules (e.g. growth factors or nutrients) are crucial parameters for the design and application of effective artificial tissue materials. Here, dynamics of selected macromolecules were studied in two different composite tissue engineering scaffolds containing an electrospun nanofiber mesh (polycaprolactone or hydrophobically plasma modified polyvinylalcohol–chitosan) encapsulated in agarose hydrogels by a conventional approach fluorescence recovery after photobleaching (FRAP) and a novel technique, raster image correlation spectroscopy (RICS). The two approaches are compared, and it is shown that FRAP is unable to determine processes occurring at low molecular concentrations, especially accurately separating binding/unbinding from diffusion, and its results depend on the concentration of the studied molecules.
    WorkplaceJ. Heyrovsky Institute of Physical Chemistry
    ContactMichaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196
    Year of Publishing2012
Number of the records: 1  

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