Source:http://linkedlifedata.com/resource/pubmed/id/10532233
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-11-2
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pubmed:abstractText |
The synthesis of hydrazinopeptides using solid-phase N-electrophilic amination was extended to the Fmoc/tert-butyl strategy. Both Boc/benzyl and Fmoc/tert-butyl strategies led to the isolation of by-products arising from the partial instability of the N-N bond during the final cleavage and deprotection step. Two paths of decomposition have been shown: the cleavage of the N-N bond leading to the regeneration of the amine and a Hofmann-type elimination yielding original dianisyl adducts. Our data suggest that the Fmoc/tert-butyl strategy is better suited for the synthesis of hydrazinopeptides.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1397-002X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
54
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
270-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10532233-Acids,
pubmed-meshheading:10532233-Amination,
pubmed-meshheading:10532233-Amino Acid Sequence,
pubmed-meshheading:10532233-Fluorenes,
pubmed-meshheading:10532233-Hydrazines,
pubmed-meshheading:10532233-Mass Spectrometry,
pubmed-meshheading:10532233-Molecular Sequence Data,
pubmed-meshheading:10532233-Peptide Biosynthesis
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pubmed:year |
1999
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pubmed:articleTitle |
Synthesis of hydrazinopeptides using solid-phase N-electrophilic amination: extension to the Fmoc/tert-butyl strategy and chemistry of the N-N bond in strong acid media.
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pubmed:affiliation |
Institut Pasteur de Lille/Institut de Biologie de Lille, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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