Layer-by-layer assembly of poly-l-lysine/hyaluronic acid protein reservoirs on poly(glycerol sebacate) surfaces
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
37924853
DOI
10.1016/j.ejpb.2023.10.023
PII: S0939-6411(23)00289-8
Knihovny.cz E-resources
- Keywords
- BMP-2 release, Bioactive protein reservoirs, Layer-by-layer coating, Poly(glycerol sebacate), Surface modification,
- MeSH
- Hyaluronic Acid * chemistry MeSH
- Layer-by-Layer Nanoparticles MeSH
- Polyelectrolytes MeSH
- Polylysine * chemistry MeSH
- Polymers MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Hyaluronic Acid * MeSH
- poly(glycerol-sebacate) MeSH Browser
- Polyelectrolytes MeSH
- Polylysine * MeSH
- Polymers MeSH
The modification of biomaterial surfaces has become increasingly relevant in the context of ongoing advancements in tissue engineering applications and the development of tissue-mimicking polymer materials. In this study, we investigated the layer-by-layer (LbL) deposition of polyelectrolyte multilayer protein reservoirs consisting of poly-l-lysine (PLL) and hyaluronic acid (HA) on the hydrophobic surface of poly(glycerol sebacate) (PGS) elastomer. Using the methods of isothermal titration calorimetry and surface plasmon resonance, we systematically investigated the interactions between the polyelectrolytes and evaluated the deposition process in real time, providing insight into the phenomena associated with film assembly. PLL/HA LbL films deposited on PGS showed an exceptional ability to incorporate bone morphogenetic protein-2 (BMP-2) compared to other growth factors tested, thus highlighting the potential of PLL/HA LbL films for osteoregenerative applications. The concentration of HA solution used for film assembly did not affect the thickness and topography of the (PLL/HA)10 films, but had a notable impact on the hydrophilicity of the PGS surface and the BMP-2 release kinetics. The release kinetics were successfully described using the Weibull model and hyperbolic tangent function, underscoring the potential of these less frequently used models to compare the protein release from LbL protein reservoirs.
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