English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

The development of hydrogels for protein delivery requires protein-hydrogelinteractions that cause minimal disruption of the protein's biologicalactivity. Biological activity can be influenced by factors such as orientationand conformation. Hydrogels must promote the adsorption of biomolecules ontothe surface and the diffusion of biomolecules into the porous network at thesurface, while maintaining native protein conformation, keeping the protein inan accessible orientation for receptor binding, and maximizing protein release.We report here the evaluation of (hydroxyethyl)methacrylate (HEMA)-basedhydrogel systems for the delivery of keratinocyte growth factor (KGF) topromote re-epithelialization in wound healing. In this work, we characterizetwo hydrogel blends in addition to HEMA alone, and report how proteinorientation, conformation, and protein release is affected. The first blendincorporates methyl methacrylate (MMA), which is known to promote adsorption ofprotein to its surface due to its hydrophobicity. The second blend incorporatesmethacrylic acid (MAA), which is known to promote the diffusion of protein intoits surface due to its hydrophilicity. We find that KGF at the surface of theHEMA/MMA blend appears to be more orientationally accessible andconformationally active than KGF at the surface of the HEMA/MAA blend. We alsoreport that KGF at the surface of the HEMA/MAA blend becomes conformationallydenatured, likely due to hydrogen bonding. While KGF at the surface of theseblends can be differentiated by FTIR-ATR spectroscopy and ToF-SIMS inconjunction with PCA, KGF swelling, uptake, and release profiles areindistinguishable. The differences in KGF orientation and conformation betweenthese blends may result in different biological responses in future cell-basedexperiments.

Differential orientation and conformation of Keratinocyte Growth Factor  observed at HEMA, HEMA/MMA, and HEMA/MAA hydrogel surfaces developed for  wound healing