In situ crosslinkable hydrogel formed from an amphiphilic amylopectin-based hydrogelator in aqueous solution was investigated with respect to its viscoelasticity, structure as well as protein encapsulation and release. Different from the physical hydrogel formed from an aqueous amylopectin system of sufficiently high concentration, such a hydrogel could be formed rapidly at room temperature and exhibit enhanced viscoelastic properties, mechanical strength, and shear thinning behavior. In addition, it has a more complex network structure with a higher fractal dimension due to intermolecular hydrophobic interactions and macromolecular chain entanglements. By circular dichroism analyses and in vitro release experiments, this hydrogel material was found to have a great potential as new matrix for the entrapment and sustained release of bovine serum albumin.
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Song et al. (2009) studied this question.
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