Source:http://linkedlifedata.com/resource/pubmed/id/10076062
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1999-3-25
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pubmed:abstractText |
Antibacterial glycopeptides isolated from insects are exciting bio-oligomers because they represent a family of compounds in which the structural and functional effects of incorporating short O-linked sugars to protein fragments can be studied. Additionally, their high activity in vitro warrants detailed further drug development efforts. Due to the limited availability of the isolated material, we used synthetic glycopeptides and some analogs to investigate the range of activity of drosocin and pyrrhocoricin. While addition of the Gal-GalNAc disaccharide to the natural mid-chain position generally increased the antibacterial activity of drosocin, pyrrhocoricin lacking sugar appeared to be more potent, with an IC50 against Escherichia coli D22 of 150 nM. Although glycosylated drosocin was active against E. coli in the low microM range in vitro, this peptide was completely inactive when injected into mice. The lack of in vivo activity of drosocin could be explained by the unusually high degradation rate of the peptides in mammalian sera. The early degradation products were inactive in vitro. In contrast, the peptides were considerably more stable in insect hemolymph, where their natural activity is manifested.
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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/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/drosocin,
http://linkedlifedata.com/resource/pubmed/chemical/pyrrhocoricin protein, Pyrrhocoris...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
1426
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
459-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10076062-Amino Acid Sequence,
pubmed-meshheading:10076062-Animals,
pubmed-meshheading:10076062-Anti-Bacterial Agents,
pubmed-meshheading:10076062-Antimicrobial Cationic Peptides,
pubmed-meshheading:10076062-Blood,
pubmed-meshheading:10076062-Drug Stability,
pubmed-meshheading:10076062-Escherichia coli,
pubmed-meshheading:10076062-Glycopeptides,
pubmed-meshheading:10076062-Hemolymph,
pubmed-meshheading:10076062-Insect Proteins,
pubmed-meshheading:10076062-Mice,
pubmed-meshheading:10076062-Microbial Sensitivity Tests,
pubmed-meshheading:10076062-Molecular Sequence Data,
pubmed-meshheading:10076062-Peptides
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pubmed:year |
1999
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pubmed:articleTitle |
Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects.
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pubmed:affiliation |
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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