Source:http://linkedlifedata.com/resource/pubmed/id/14531666
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
41
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pubmed:dateCreated |
2003-10-8
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pubmed:abstractText |
Proteins are functional biopolymers; viewed as molecules, they are also monodisperse polyamides with chemically reactive side chains. This paper describes the use of proteins as starting materials for the synthesis of monodisperse polymers with nonbiological functionalities attached to the side chains. It demonstrates the complete derivatization of amine groups (lysine side chains and N-termini) on three different proteins by addition of activated carboxylate reagents in aqueous solutions containing sodium dedecyl sulfate (SDS), under denaturing conditions. Several different acylating reagents were used to generate derivatized proteins; the resulting compounds constitute a new class of monodisperse, semisynthetic polymers, having the potential for wide variation in the structure of the backbone and of the side chains. Modification of lysozyme on a gram scale demonstrated that the method can generate useful quantities of material.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetic Anhydrides,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrase II,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/acetic anhydride
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
125
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12392-3
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pubmed:dateRevised |
2008-1-17
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pubmed:meshHeading |
pubmed-meshheading:14531666-Acetic Anhydrides,
pubmed-meshheading:14531666-Acetylation,
pubmed-meshheading:14531666-Animals,
pubmed-meshheading:14531666-Carbonic Anhydrase II,
pubmed-meshheading:14531666-Cattle,
pubmed-meshheading:14531666-Lysine,
pubmed-meshheading:14531666-Muramidase,
pubmed-meshheading:14531666-Polymers,
pubmed-meshheading:14531666-Proteins,
pubmed-meshheading:14531666-Ubiquitin
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pubmed:year |
2003
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pubmed:articleTitle |
Synthesis of monodisperse polymers from proteins.
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pubmed:affiliation |
Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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