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Protein-Cross-Linked Hydrogels with Tailored Swelling and Bioactivity Performance: A Comparative Study
journal contribution
posted on 2016-11-02, 00:00 authored by Bin Li, Kaixuan Ren, Yupeng Wang, Yanxin Qi, Xuesi Chen, Yubin HuangThe
design of protein-based hydrogels that include biological activity
independent of structural functionality is desirable for many bioengineering
applications. Here a general route for construction of protein-based
hydrogel is proposed by pretreatment of protein with thiolation agent
and succeeding conjugation with 4-arm PEG-acrylate via Michael addition
reaction. Different swelling behaviors responding to temperature and
ions are comparatively studied for hydrogel cross-linked with hemoglobin
(multimeric protein), albumin (monomeric protein), and dithiothreitol
(DTT, small molecule). Meanwhile, the microscopic structure change
is studied to correlate with the macroscopic hydrogel swelling behavior.
Results show that proteins, which function as multisite cross-linkers,
affect the gel swelling behaviors, and the effect is more profound
for multimeric proteins when exposed to stimulus for protein dissociation.
Moreover, the catalytic activity derived from hemoglobin is also preserved
in the hydrogel, as demonstrated by the successfully synthesis of
the colored product. By taking advantage of each particular protein,
a broad range of functional materials can be expected for potential
biomedical applications, such as stimuli-responsive hydrogel and immobilized
enzyme.
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Bioactivity PerformanceMichael addition reactionstimuli-responsive hydrogelmacroscopic hydrogelDTTProtein-Cross-Linked Hydrogelsmultimeric proteinsResults show4- arm PEG-acrylateComparative Studybioengineering applicationsmultisite cross-linkershydrogel cross-linkedprotein-based hydrogelsprotein dissociationstructure changeprotein-based hydrogelthiolation agent
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