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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-6-3
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pubmed:abstractText |
Mass spectrometry (MS) analysis is applicable to a broad range of biological analytes and has the important advantage that it does not require analytes to be labeled. A drawback of MS methods, however, is the need for chromatographic steps to prepare the analyte, precluding MS from being used in chemical screening and rapid analysis. Here, we report that surfaces that are chemically tailored for characterization by matrix-assisted laser-desorption ionization time-of-flight MS eliminate the need for sample processing and make this technique adaptable to parallel screening experiments. The tailored substrates are based on self-assembled monolayers that present ligands that interact with target proteins and enzymes. We apply this method to screen a chemical library against protease activity of anthrax lethal factor, and report a compound that inhibits lethal factor activity with a K(i) of 1.1 microM and blocks the cleavage of MEK1 in 293 cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/MAP2K1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/anthrax toxin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1087-0156
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
717-23
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15146199-Antigens, Bacterial,
pubmed-meshheading:15146199-Apoptosis,
pubmed-meshheading:15146199-Bacterial Toxins,
pubmed-meshheading:15146199-Blotting, Western,
pubmed-meshheading:15146199-Cell Differentiation,
pubmed-meshheading:15146199-Cell Line,
pubmed-meshheading:15146199-Cell Line, Tumor,
pubmed-meshheading:15146199-Cell Survival,
pubmed-meshheading:15146199-Dose-Response Relationship, Drug,
pubmed-meshheading:15146199-Drug Evaluation, Preclinical,
pubmed-meshheading:15146199-Enzyme Inhibitors,
pubmed-meshheading:15146199-Hemagglutinins,
pubmed-meshheading:15146199-Humans,
pubmed-meshheading:15146199-Kinetics,
pubmed-meshheading:15146199-Lipopolysaccharides,
pubmed-meshheading:15146199-MAP Kinase Kinase 1,
pubmed-meshheading:15146199-Macrophages,
pubmed-meshheading:15146199-Peptides,
pubmed-meshheading:15146199-Recombinant Fusion Proteins,
pubmed-meshheading:15146199-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15146199-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor.
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pubmed:affiliation |
Department of Chemistry, Institute for Biophysical Dynamics, The University of Chicago, Illinois 60637, 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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