2008
DOI: 10.1002/adfm.200701288
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Protein‐Based Hydrogels with Tunable Dynamic Responses

Abstract: Development of hydrogel materials that respond to specific stimuli has been of significant interest in the design of modern functional materials. A variety of previous studies have used the ligand‐binding capability of proteins to design hydrogels that change their crosslinking density in response to stimuli. However, these materials generally undergo relatively small dynamic response, with limited control over response characteristics. This manuscript describes an alternative approach that exploits the abilit… Show more

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Cited by 88 publications
(91 citation statements)
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“…[ 38,39 ] For silk protein based hydrogels, the β-sheet structure serves as crosslinking sites, which gives rise to the gel network formation and immobilize the molecular chain throughout the whole hydrogels. Our work illuminated that intermolecular β-sheet structure of RSF molecules may be essential for the hydrogel network, thus, the differences between β-sheet structure in the mechanically strong RSF/HPMC9 hydrogel and that of in pure RSF hydrogel should be focused.…”
Section: Size Of the Crosslinking Sites Of The Rsf/hpmc9 Hydrogelmentioning
confidence: 99%
“…[ 38,39 ] For silk protein based hydrogels, the β-sheet structure serves as crosslinking sites, which gives rise to the gel network formation and immobilize the molecular chain throughout the whole hydrogels. Our work illuminated that intermolecular β-sheet structure of RSF molecules may be essential for the hydrogel network, thus, the differences between β-sheet structure in the mechanically strong RSF/HPMC9 hydrogel and that of in pure RSF hydrogel should be focused.…”
Section: Size Of the Crosslinking Sites Of The Rsf/hpmc9 Hydrogelmentioning
confidence: 99%
“…Specifically, our approach relies on a ligand-induced protein conformational change to induce changes in hydrogel properties. In our general approach, which has been detailed previously, [5][6][7] In this study we formed and characterized dynamic hydrogel microspheres in which a protein conformational change was used to control microsphere volume changes and the release of an encapsulated drug. In particular, a specific biochemical ligand, trifluoperazine, induced calmodulin's nanometer scale conformation change, which translated to a 48.7% microsphere volume decrease.…”
Section: Introductionmentioning
confidence: 99%
“…PEG-CaM-PEG conjugates were synthesized, purified, and characterized as previously described. [5][6][7] PEG 575 -CaM-PEG 575 microspheres were formed using a water-in-oil emulsion polymerization in an Argon environment. The same process was repeated with a different water phase containing PEGDA 575 to form PEG 575 microspheres.…”
Section: Introductionmentioning
confidence: 99%
“…In the presence of trifluoperazine, the CaM-containing hydrogels underwent a significant decrease in volume, demonstrating that a nanometer-scale protein conformational change can be translated into macroscopic changes in material properties. More recently, REVIEW www.advmat.de CaM-based materials have been photopolymerized to create materials that undergo substantial (more than five-fold), reversible volume changes, which can be used to synthesize spatially patterned actuators, [154] tunable optical biosensors, [173] and dynamic growth-factor delivery systems [174] (Fig. 8).…”
Section: Allosteric Protein Conformational Changes In Materialsmentioning
confidence: 99%