Macromol. Biosci. 9/2009

Ehrick, Jason D.; Luckett, Matthew R.; Khatwani, Santoshkumar L.; Wei, Yinan; Deo, Sapna K.; Bachas, Leonidas G.; Daunert, Sylvia

doi:10.1002/mabi.200990017

Cited by 15 publications

(26 citation statements)

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“…This new mechanism may be broadly adaptable as there are over 200 proteins that undergo well characterized ligand-responsive conformation changes, [14] and proteins can be readily engineered using recombinant techniques to tailor their responsiveness. [15] In addition, researchers have recently created other dynamic hydrogels based on proteins that can undergo conformational changes, [16][17][18] and these other systems could be candidates for bio-responsive protein release as well. Therefore, the approach demonstrated here could provide a broad mechanism to control the release of therapeutic proteins.…”

Section: Resultsmentioning

confidence: 99%

Triggered Drug Release from Dynamic Microspheres via a Protein Conformational Change

King¹,

Pytel²,

Ng³

et al. 2010

Macromolecular Bioscience

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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. This specific, ligand‐induced volume change triggered the release of a model drug, vascular endothelial growth factor (VEGF), at pre‐determined times. After release from the microspheres, 85.6 ± 10.5% of VEGF was in its native conformation. Taken together, these results suggest that protein conformational change could serve as a useful mechanism to control drug release from dynamic hydrogels.magnified image

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Section: Resultsmentioning

confidence: 99%

Triggered Drug Release from Dynamic Microspheres via a Protein Conformational Change

King¹,

Pytel²,

Ng³

et al. 2010

Macromolecular Bioscience

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“…This hydrogel design concept of linking allosterically regulated proteins directly to chemical polymers is likely generically applicable as described in a recent study by Ehrick et al at the example of a glucose‐responsive biohybrid material. As a sensor molecule, the E. coli ‐derived glucose/galactose‐binding protein (GBP) was used.…”

Section: Stimulus‐sensing Biohybrid Hydrogels Based On Inducible Confmentioning

confidence: 97%

Design, Synthesis, and Application of Stimulus‐Sensing Biohybrid Hydrogels

Hotz

Wilcke

Weber

2013

Macromol. Rapid Commun

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A key feature of any living system is the ability to sense and react to the environmental stimuli. The biochemical characterization of the underlying biological sensors combined with advances in polymer chemistry has enabled the development of stimulus-sensitive biohybrid materials that translate most diverse chemical and biological input into a precise change in material properties. In this review article, we first describe synthesis strategies of how biological and chemical polymers can functionally be interconnected. We then provide a comprehensive overview of how the different properties of biological sensor molecules such as competitive target binding and allosteric modulation can be harnessed to develop responsive materials with applications in tissue engineering and drug delivery.

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“…The ability of glucose-binding protein to undergo a conformational change that triggers a change in gel size and porosity has been demonstrated, 198 where the change in gel linear dimension is 2-3%. Gels crosslinked with metallothioneins 199 show decrease in volume down to 20% of the original (change in linear dimension of 58% of the original) owing to a very large change from an unfolded to a folded state of the protein in response to heavy metal FEATURE ARTICLE ions.…”

Section: Hydrogels With Biological Recognition Propertiesmentioning

confidence: 99%

Physics of engineered protein hydrogels

Kim

Tang

Olsen

2013

J Polym Sci B Polym Phys

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Artificially engineered proteins and synthetic polypeptides have attracted widespread interest as building blocks for polymer hydrogels. The biophysical properties of the proteins, such as molecular recognition abilities, folded chain structures, and sequence-dependent thermodynamic behavior, enable advances in functional, responsive, and tunable gels. This review discusses the design of polymer hydrogels that incorporate protein domains, highlighting new challenges in polymer physics that are presented by this emerging class of materials. Five types of engineered protein hydrogels are discussed: (a) physically associating protein polymer gels, (b) amorphous artificially engineered protein networks, (c) engineered proteins with crystalline domains, (d) stretchable protein tertiary structures in gels, and (e) protein gels with biological recognition properties. The physics of the protein component and the physical properties of the resulting hydrogels are summarized, illustrating how advances in understanding these systems are leading to exciting novel biofunctional hydrogels.

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Macromol. Biosci. 9/2009

Cited by 15 publications

References 0 publications

Triggered Drug Release from Dynamic Microspheres via a Protein Conformational Change

Triggered Drug Release from Dynamic Microspheres via a Protein Conformational Change

Design, Synthesis, and Application of Stimulus‐Sensing Biohybrid Hydrogels

Physics of engineered protein hydrogels

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