Source:http://linkedlifedata.com/resource/pubmed/id/18067155
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2008-4-2
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pubmed:abstractText |
The conformational transition of molecular chains of regenerated silk fibroin (SF) aqueous solution is systematically investigated by circular dichroism, Raman, IR, and UV-vis spectroscopies. It is found that an initial random coil conformation of the SF can be readily changed into an ordered beta-sheet structure by optimizing the solution conditions, such as the SF concentration, pH, temperature, or metal-ion content. Circular dichroic spectra quantitatively confirm a steadily decreased content of the random coil conformation but a significantly increased beta-sheet content after an ultrasonic or extruding treatment. Furthermore, the extrusion is more powerful to achieve high beta-sheet content than the ultrasonic. It is interesting that the polarized optical micrographs of the SF aqueous solution extruded by injection illustrate the formation and existence of liquid crystalline state. A study of extrusion in vitro could be used as a model system to understand the natural silk spinning process in silkworm.
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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/Fibroins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/fibroin, silkworm
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3525
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
497-505
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18067155-Animals,
pubmed-meshheading:18067155-Bombyx,
pubmed-meshheading:18067155-Fibroins,
pubmed-meshheading:18067155-Hot Temperature,
pubmed-meshheading:18067155-Insect Proteins,
pubmed-meshheading:18067155-Ions,
pubmed-meshheading:18067155-Liquid Crystals,
pubmed-meshheading:18067155-Metals,
pubmed-meshheading:18067155-Models, Chemical,
pubmed-meshheading:18067155-Protein Structure, Secondary,
pubmed-meshheading:18067155-Spectrum Analysis,
pubmed-meshheading:18067155-Water
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pubmed:year |
2008
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pubmed:articleTitle |
Conformational transition and liquid crystalline state of regenerated silk fibroin in water.
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pubmed:affiliation |
Institute of Materials Chemistry, Key Laboratory of Advanced Civil Engineering Materials, College of Materials Science and Engineering, Tongji University, 1239 Siping Road, Shanghai 200092, China. adamxgli@yahoo.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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