Source:http://linkedlifedata.com/resource/pubmed/id/19224560
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2009-4-27
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pubmed:abstractText |
We report the assembly of seven different antibodies (and two antigens) into functional supramolecular structures that are specifically designed to facilitate integration into devices using entirely biologically based bottom-up fabrication. This is enabled by the creation of an engineered IgG-binding domain (HG3T) with an N-terminal hexahistidine tag that facilitates purification and a C-terminal enzyme-activatable pentatyrosine "pro-tag" that facilitates covalent coupling to the pH stimuli-responsive polysaccharide, chitosan. Because we confer pH-stimuli responsiveness to the IgG-binding domain, it can be electrodeposited or otherwise assembled into many configurations. Importantly, we demonstrate the loading of both HG3T and antibodies can be achieved in a linear fashion so that quantitative assessment of antibodies and antigens is feasible. Our demonstration formats include: conventional multiwell plates, micropatterned electrodes, and fiber networks. We believe biologically based fabrication (i.e., biofabrication) provides bottom-up hierarchical assembly of a variety of nanoscale components for applications that range from point-of-care diagnostics to smart fabrics.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Chitosan,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1097-0290
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pubmed:author |
pubmed-author:BentleyWilliam EWE,
pubmed-author:DeShongPhilipP,
pubmed-author:FernandesRohanR,
pubmed-author:HungChi-WeiCW,
pubmed-author:KobatakeEiryE,
pubmed-author:LewandowskiAngela TAT,
pubmed-author:PayneGregory FGF,
pubmed-author:ShiXiao-WenXW,
pubmed-author:TsaoChen-YuCY,
pubmed-author:ValdesJames JJJ,
pubmed-author:WuHsuan-ChenHC
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pubmed:copyrightInfo |
Copyright 2008 Wiley Periodicals, Inc.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
231-40
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pubmed:meshHeading |
pubmed-meshheading:19224560-Amino Acid Motifs,
pubmed-meshheading:19224560-Antibodies,
pubmed-meshheading:19224560-Antigens,
pubmed-meshheading:19224560-Binding Sites,
pubmed-meshheading:19224560-Biotechnology,
pubmed-meshheading:19224560-Chitosan,
pubmed-meshheading:19224560-Hydrogen-Ion Concentration,
pubmed-meshheading:19224560-Macromolecular Substances,
pubmed-meshheading:19224560-Protein Binding,
pubmed-meshheading:19224560-Recombinant Fusion Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Biofabrication of antibodies and antigens via IgG-binding domain engineered with activatable pentatyrosine pro-tag.
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pubmed:affiliation |
Center for Biosystems Research, University of Maryland Biotechnology Institute, College Park, Maryland 20742, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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