Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/42489

TitleInfluence of the sulfation degree of glycosaminoglycans on their multilayer assembly with poly-L-lysine
Author(s)Teixeira, Raquel
Reis, R. L.
Pashkuleva, I.
KeywordsLbL films
Hyaluronan
Chondroitin sulfate
Heparin
Multi-parametric surface plasmon resonance
Quartz-crystal microbalance
Electrokinetic analysis
Viscoelastic properties
Refractive index
Hydration
Issue dateMay-2016
PublisherElsevier
JournalColloids and Surfaces B: Biointerfaces
CitationTeixeira R., Reis R. L., Pashkuleva I. Influence of the sulfation degree of glycosaminoglycans on their multilayer assembly with poly-L-lysine, Colloids and Surfaces B: Biointerfaces, Vol. 145, pp. 567-575, doi:10.1016/j.colsurfb.2016.05.069, 2016
Abstract(s)We report on the build-up and the intrinsic properties of polyelectrolyte multilayer films from poly-L-lysine and glycosaminoglycans (GAGs) with different sulfation degree, i.e. different charge. We used three complementary techniques, namely electrokinetic analysis (EKA), quartz-crystal microbalance with dissipation (QCM-D) and surface plasmon resonance (SPR), to characterize the assembly process and to assess the properties of the obtained films. EKA elucidated the contribution of the polymers charged groups to the net surface charge of the films and suggested that the assembly process is not solely driven by electrostatic interactions. The combined analysis of QCM-D and SPR data demonstrated that the mechanical properties of the films are dependent on the polymer charge: sulfated GAGs (heparin and chondroitin sulfate) form elastic films while hyaluronan (no sulfation) assembles into multilayer constructs with viscous behavior. The contribution of the water content to these distinct regimes is also discussed. Finally, we show that rather complete characterization of the film properties is possible by SPR employing the two-wavelength and two-media approach: thickness, adsorbed mass, refractive index, and interaction kinetics of the assembly process can be studied by SPR alone.
TypeArticle
URIhttp://hdl.handle.net/1822/42489
DOI10.1016/j.colsurfb.2016.05.069
ISSN0927-7765
Publisher versionhttp://www.sciencedirect.com/science/article/pii/S0927776516304052
Peer-Reviewedyes
AccessRestricted access (UMinho)
Appears in Collections:3B’s - Artigos em revistas/Papers in scientific journals

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