Source:http://linkedlifedata.com/resource/pubmed/id/19296655
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2009-4-13
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pubmed:abstractText |
The use of proteins as monomers for materials assembly enables customization of chemical, physical, and functional properties. However, natural materials-forming proteins are difficult to produce as recombinant protein monomers and require harsh conditions to initiate assembly. We have generated materials using the recombinant transcription factor Ultrabithorax, a Drosophila melanogaster protein not known or anticipated to form extended oligomers in vivo. Ultrabithorax self-assembles at the air-water interface into nanoscale fibers, which further associate to form macroscale films, sheets, ropes, and tethered encapsulates. These materials self-adhere, allowing construction of more complex architectures. The Ultrabithorax sequence contains two regions capable of generating materials, only one of which contains motifs found in elastomeric proteins. However, both minimal regions must be included to produce robust materials. Relative to other protein-based materials, Ultrabithorax assembles at significantly reduced concentrations, on faster timescales, and under gentler conditions, properties that facilitate future materials engineering and functionalization.
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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/Biocompatible Materials,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubx protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1526-4602
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
829-37
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pubmed:meshHeading |
pubmed-meshheading:19296655-Animals,
pubmed-meshheading:19296655-Biocompatible Materials,
pubmed-meshheading:19296655-Blotting, Western,
pubmed-meshheading:19296655-DNA,
pubmed-meshheading:19296655-Drosophila Proteins,
pubmed-meshheading:19296655-Drosophila melanogaster,
pubmed-meshheading:19296655-Elastic Tissue,
pubmed-meshheading:19296655-Homeodomain Proteins,
pubmed-meshheading:19296655-Macromolecular Substances,
pubmed-meshheading:19296655-Materials Testing,
pubmed-meshheading:19296655-Protein Interaction Domains and Motifs,
pubmed-meshheading:19296655-Stress, Mechanical,
pubmed-meshheading:19296655-Transcription Factors
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pubmed:year |
2009
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pubmed:articleTitle |
The Drosophila transcription factor ultrabithorax self-assembles into protein-based biomaterials with multiple morphologies.
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pubmed:affiliation |
Department of Biochemistry and Cell Biology, Rice University, 6100 South Main Street, Houston, Texas 77005, 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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