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.
GRAPHICAL ABSTRACT
![](/cms/asset/6bc529e1-1514-4668-9d73-48cf20f50206/gpom_a_1074904_uf0001_oc.jpg)
Acknowledgments
The authors would like to thank A. Hernandez-Garcia for providing the (Lys)6-encoding dsDNA adapter and M. W. T. Werten for genetic cloning/fermentation.