ArticleRSC advances2021
Encapsulation of BSA in hybrid PEG hydrogels: stability and controlled release.
Article in RSC advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Recent advances in polymer-based drug delivery systems for atopic dermatitis: enhancing therapeutic efficacy and outcomes.Materials today. Bio · 2025Review
- Albumin as a natural and moldable biomaterial for biomimetic drug delivery applications.International journal of pharmaceutics · 2025Review
- Role of Polymer Concentration on the Release Rates of Proteins from Single- and Double-Network Hydrogels.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hybrid hydrogels based on silylated polyethylene glycol, Si-PEG, were evaluated as hybrid matrices able to trap, stabilize and release bovine serum albumin (BSA) in a controlled manner. Parameters of the inorganic condensation reaction leading to a siloxane (Si-O-Si) three dimensional network were carefully investigated, in particular the temperature, the surrounding hygrometry and the Si-PEG concentration. The resulting hydrogel structural features affected the stability, swelling, and mechanical properties of the network, leading to different protein release profiles. Elongated polymer assemblies were observed, the length of which ranged from 150 nm to over 5 μm. The length could be correlated to the Si-O-Si condensation rate from 60% (hydrogels obtained at 24 °C) to about 90% (xerogels obtained at 24 °C), respectively. Consequently, the controlled release of BSA could be achieved from hours to several weeks, with respect to the fibers' length and the condensation rate. The protein stability was evaluated by means of a thermal study. The main results gave insight into the biomolecule structure preservation during polymerisation, with Δ
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Registered trials
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