The conditions determining network-forming and aggregation properties of hyaluronan on the mica surface were studied. The hyaluronan was deposited on the surface from aqueous and saline solutions and attached by a bivalent cation. The morphology of the immobilized assemblies was characterized by atomic force microscopy. The experimental results show that the morphology and size of the aggregates as well as the density of the interconnecting fibrillar network, both made of hyaluronan, at the liquid-solid phase interface are determined not only by its molecular weight or concentration in solution, but also by the dissolution conditions and storage time. These findings extend the current state of knowledge about the conformational variability of this biologically important polymer. Understanding the conformational variability is of great importance, as it governs the physiological functions of hyaluronan, as well as its processability and formulations. That in turn determines its usability in different pharmacological and biomaterial applications.
- MeSH
- hydrofobní a hydrofilní interakce MeSH
- hypertonický solný roztok chemie MeSH
- kyselina hyaluronová chemie MeSH
- mikroskopie atomárních sil metody MeSH
- molekulární struktura MeSH
- molekulová hmotnost MeSH
- polymery chemie MeSH
- povrchové vlastnosti MeSH
- rozpustnost MeSH
- silikáty hliníku chemie MeSH
- skladování léků MeSH
- voda chemie MeSH
- vodíková vazba MeSH
- Publikační typ
- časopisecké články MeSH
Atomically flat mica surfaces were chemically modified with an alkyl trifluoromethyl ketone, a covalent inhibitor of esterase 2 from Alicyclobacillus acidocaldarius, which served as a tag for ligand-directed immobilization of esterase-linked proteins. Purified NADH oxidase from Thermus thermophilus and human exportin-t from cell lysates were anchored on the modified surfaces. The immobilization effectiveness of the proteins was studied by atomic force microscopy (AFM). It was shown that ligand-esterase interaction allowed specific attachment of exportin-t and resulted in high-resolution images and coverage patterns that were comparable with immobilized purified protein. Moreover, the biological functionality of immobilized human exportin-t in forming a quaternary complex with tRNA and the GTPase Ran-GTP, and the dimension changes before and after complex formation were also determined by AFM.
- MeSH
- bakteriální proteiny MeSH
- esterasy MeSH
- exprese genu MeSH
- financování organizované MeSH
- ketony farmakologie chemie MeSH
- lidé MeSH
- ligandy MeSH
- mikroskopie atomárních sil MeSH
- multienzymové komplexy genetika chemie MeSH
- NADH, NADPH oxidoreduktasy genetika chemie MeSH
- nukleocytoplazmatické transportní proteiny genetika chemie MeSH
- rekombinantní fúzní proteiny genetika chemie ultrastruktura MeSH
- silikáty hliníku chemie MeSH
- terciární struktura proteinů MeSH
- Thermus thermophilus enzymologie MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
