Abstract
Functionalization of xanthan hydrogels is of interest for biomaterial applications. The authors report characterization of electrostatic complexation of xanthan with a recombinant collagen-inspired triblock protein polymer. This polymer has one charged polylysine end-block that can bind to xanthan by electrostatic interactions, and another end-block that can self-assemble into thermosensitive collagen-like triple helices; the end-blocks are connected by a neutral, hydrophilic, mostly inert random coil. The protein modifies the xanthan/protein composite hydrogels in three ways: (a) a significant increase in storage modulus, (b) thermosensitivity, and (c) a two-step strain softening in nonlinear rheology.
Original language | English |
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Pages (from-to) | 125-133 |
Journal | International Journal of Polymeric Materials and Polymeric Biomaterials |
Volume | 65 |
Issue number | 3 |
DOIs | |
Publication status | Published - 11 Feb 2016 |
Keywords
- collagen-inspired protein
- composite hydrogels
- electrostatic interaction
- strain-softening
- thermosensitivity
- Xanthan