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[[Image:BR_Hydrogel.jpg|thumb|400px|right| We have engineered the beta roll peptide to self-assemble upon addition of calcium.  We have combined this with a self-assembling alpha-helical peptide to create a calcium-dependent hydrogel-forming biomaterial.]]


'''Bifunctional Proteinaceous Hydrogels for Bioelectrocatalysis'''


Self-assembly is an essential process for all forms of life.  For example, proteins spontaneously fold into well-defined 3-dimensional structures, and cellular organelles form that spatially segregate diverse cellular processes.  As engineers aim to create  new devices and systems at ever decreasing size scales, self-assembly processes become increaseingly attactive techniques.
'''Self-Assembling Protein Hydrogels for Bioelectrocatalysis'''


We are collaborating with Plamen Atanassov at University of New Mexico, Scott Calabrese-Barton at Michigan State University and Shelley Minteer at Saint Louis University to make improved electrodes for biofuel cells.  In a biofuel cell, redox enzymes are immobilized on electrode surfaces.  Enzymes located at the anode are able to oxidize substrates and the electrons move through an external circuit to create power.  On the cathode, other redox enzymes are able to use the electrons to reduce oxygen to water.  The net result of this process is the generation of electricity from a variety of readily available biofuel sources, with oxygen as the terminal electron acceptor.
Self-assembly is an essential process for all forms of life.  For example, proteins spontaneously fold into well-defined 3-dimensional structures, and cellular organelles form that spatially segregate diverse cellular processes.  As engineers aim to create new devices and systems at ever decreasing size scales, self-assembly processes become increasingly attractive techniques.


The architecture of the electrodes is crucial for biofuel cell performance.  The enzymes on the electrodes must be positioned so that electrons can easily move between the enzymatic active site and the electorde surface (Direct Electron Transfer (DET)).  Alternatively, the enzymes can be immoblilized with redox mediators, such as osmium, that facilitate the transport of electrons from the electrodes to the enzymes (Fig. 1).  In this Mediated Electron Transport (MET) configuration, the enzyme and mediators are immobilized in a polymer matrix on the electrode surface.  While this system has been used to demonstrate impressive biofuel cell performances, it is potentially hampered by poor dispersion of the enzyme and mediator within the polymer matrix, and complex manufacturing requirments.
We are interested in using protein self-assembly in bioelectrocatalytic applications including biofuel cells and biosensors.  In these devices it is critical to have a high loading of enzymes on the electrode and to address transport issues including electrical communication with the electrode and substrate and product transport to and from the enzyme.


We are using biological self-assembly to improve the biofuel cell electrode construction and performance (Fig. 2).  Instead of combing enzymes and mediators in a polymer matrix, we are creating self-assembling protein-based hydrogels that intrinsically include the redox enzymes and the mediators.  In this configuration the loading of the enzyme and the mediators into the hydrogel can be finely controlled, and the hydrogel assembly process will be well-defined and repeatable.  These new bioelectrocatalytic hydrogels will have the potential to significantly improve biofuel cell performance.
We have developed a technology where self-assembly domains are genetically appended to globular proteins and this enables the proteins to self-assemble into bifunctional hydrogels.  We have performed this modification on over a dozen different proteins and in all cases the proteins retain their biological function (activity) while gaining the ability to form a biomaterial.  We have demonstrated the use of these materials as electrode modifications for biofuel cells and biosensors.  For example, we have created a hydrogel composed of three dehydrogenase enzymes that are able to form a metabolic pathway for the oxidation of methanol to carbon dioxide.  This protein hydrogel was then used to make an enzyamtic biofuel cell. We are continuing to develop this approach to make catalytic biomaterials for additional applications.


   
In our original protein hydrogels we used self-assembling alpha-helical appendages as cross-linking domains. We have now engineered the calcium-dependent beta roll domain to serve as a calcium-dependent cross-linking motif.  This allows for hydrogel formation to be controlled by calcium addition.


'''Related Publications'''
'''Related Publications'''


<biblio>
<biblio>
#Paper4 pmid=19061242
#Paper8 pmid=23239008
#Paper7 pmid=22545587
#Paper6 pmid=20457694
#Paper5 pmid=20420519
#Paper4 pmid=19577577
#Paper3 pmid=18824691
#Paper3 pmid=18824691
#Paper2 pmid=18096378
#Paper2 pmid=18096378
#Paper1 pmid=17887795  
#Paper1 pmid=17887795  
</biblio>
</biblio>

Revision as of 12:53, 17 July 2014

Banta Lab

Protein and Metabolic Engineering

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We have engineered the beta roll peptide to self-assemble upon addition of calcium. We have combined this with a self-assembling alpha-helical peptide to create a calcium-dependent hydrogel-forming biomaterial.


Self-Assembling Protein Hydrogels for Bioelectrocatalysis

Self-assembly is an essential process for all forms of life. For example, proteins spontaneously fold into well-defined 3-dimensional structures, and cellular organelles form that spatially segregate diverse cellular processes. As engineers aim to create new devices and systems at ever decreasing size scales, self-assembly processes become increasingly attractive techniques.

We are interested in using protein self-assembly in bioelectrocatalytic applications including biofuel cells and biosensors. In these devices it is critical to have a high loading of enzymes on the electrode and to address transport issues including electrical communication with the electrode and substrate and product transport to and from the enzyme.

We have developed a technology where self-assembly domains are genetically appended to globular proteins and this enables the proteins to self-assemble into bifunctional hydrogels. We have performed this modification on over a dozen different proteins and in all cases the proteins retain their biological function (activity) while gaining the ability to form a biomaterial. We have demonstrated the use of these materials as electrode modifications for biofuel cells and biosensors. For example, we have created a hydrogel composed of three dehydrogenase enzymes that are able to form a metabolic pathway for the oxidation of methanol to carbon dioxide. This protein hydrogel was then used to make an enzyamtic biofuel cell. We are continuing to develop this approach to make catalytic biomaterials for additional applications.

In our original protein hydrogels we used self-assembling alpha-helical appendages as cross-linking domains. We have now engineered the calcium-dependent beta roll domain to serve as a calcium-dependent cross-linking motif. This allows for hydrogel formation to be controlled by calcium addition.

Related Publications

  1. Kim YH, Campbell E, Yu J, Minteer SD, and Banta S. Complete oxidation of methanol in biobattery devices using a hydrogel created from three modified dehydrogenases. Angew Chem Int Ed Engl. 2013 Jan 28;52(5):1437-40. DOI:10.1002/anie.201207423 | PubMed ID:23239008 | HubMed [Paper8]
  2. Dooley K, Kim YH, Lu HD, Tu R, and Banta S. Engineering of an environmentally responsive beta roll peptide for use as a calcium-dependent cross-linking domain for peptide hydrogel formation. Biomacromolecules. 2012 Jun 11;13(6):1758-64. DOI:10.1021/bm3002446 | PubMed ID:22545587 | HubMed [Paper7]
  3. Lu HD, Wheeldon IR, and Banta S. Catalytic biomaterials: engineering organophosphate hydrolase to form self-assembling enzymatic hydrogels. Protein Eng Des Sel. 2010 Jul;23(7):559-66. DOI:10.1093/protein/gzq026 | PubMed ID:20457694 | HubMed [Paper6]
  4. Banta S, Wheeldon IR, and Blenner M. Protein engineering in the development of functional hydrogels. Annu Rev Biomed Eng. 2010 Aug 15;12:167-86. DOI:10.1146/annurev-bioeng-070909-105334 | PubMed ID:20420519 | HubMed [Paper5]
  5. Wheeldon IR, Campbell E, and Banta S. A chimeric fusion protein engineered with disparate functionalities-enzymatic activity and self-assembly. J Mol Biol. 2009 Sep 11;392(1):129-42. DOI:10.1016/j.jmb.2009.06.075 | PubMed ID:19577577 | HubMed [Paper4]
  6. Wheeldon IR, Gallaway JW, Barton SC, and Banta S. Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks. Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15275-80. DOI:10.1073/pnas.0805249105 | PubMed ID:18824691 | HubMed [Paper3]
  7. Gallaway J, Wheeldon I, Rincon R, Atanassov P, Banta S, and Barton SC. Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor. Biosens Bioelectron. 2008 Mar 14;23(8):1229-35. DOI:10.1016/j.bios.2007.11.004 | PubMed ID:18096378 | HubMed [Paper2]
  8. Wheeldon IR, Barton SC, and Banta S. Bioactive proteinaceous hydrogels from designed bifunctional building blocks. Biomacromolecules. 2007 Oct;8(10):2990-4. DOI:10.1021/bm700858p | PubMed ID:17887795 | HubMed [Paper1]

All Medline abstracts: PubMed | HubMed

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