Source:http://linkedlifedata.com/resource/pubmed/id/11710049
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-11-16
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pubmed:abstractText |
Hybrid hydrogels of hydrophilic synthetic polymers cross-linked by protein modules undergo externally triggered volume transitions as a result of protein conformational changes. To investigate the influence of coiled-coil protein structure and stability on hydrogel volume transition, a series of block proteins containing interspersed naturally derived recombinant coiled-coils was synthesized. Proteins were characterized using circular dichroism, size exclusion chromatography, gel electrophoresis, and analytical ultracentrifugation. The block proteins formed self-associating oligomers and displayed thermal unfolding profiles indicative of a hierarchic higher-order structure. Hybrid hydrogels were assembled from an N-(2-hydroxypropyl)-methacrylamide (HPMA) copolymer and His-tagged block proteins through metal complexation. A temperature-induced decrease in hydrogel swelling was observed, and the onset temperature of the volume transition corresponded to the onset temperature of protein unfolding. We conclude that stimuli-responsive properties of hybrid hydrogels can be tailored by engineering the structure and properties of protein cross-links.
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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/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogels,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1525-7797
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
912-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11710049-Amino Acid Sequence,
pubmed-meshheading:11710049-Base Sequence,
pubmed-meshheading:11710049-Biopolymers,
pubmed-meshheading:11710049-Cross-Linking Reagents,
pubmed-meshheading:11710049-DNA, Recombinant,
pubmed-meshheading:11710049-Drug Stability,
pubmed-meshheading:11710049-Hydrogels,
pubmed-meshheading:11710049-Macromolecular Substances,
pubmed-meshheading:11710049-Models, Molecular,
pubmed-meshheading:11710049-Molecular Sequence Data,
pubmed-meshheading:11710049-Protein Conformation,
pubmed-meshheading:11710049-Protein Denaturation,
pubmed-meshheading:11710049-Protein Engineering,
pubmed-meshheading:11710049-Protein Structure, Secondary,
pubmed-meshheading:11710049-Recombinant Proteins,
pubmed-meshheading:11710049-Thermodynamics
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pubmed:year |
2001
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pubmed:articleTitle |
Hybrid hydrogels cross-linked by genetically engineered coiled-coil block proteins.
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pubmed:affiliation |
Departments of Bioengineering and Pharmaceutics and Pharmaceutical Chemistry, University of Utah, Salt Lake City, Utah 84112, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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