Source:http://linkedlifedata.com/resource/pubmed/id/20673224
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2010-10-27
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pubmed:abstractText |
We have synthesized a series of short peptides (17 to 20 amino acids), originally derived from Limulus anti-lipopolysaccharide factor LALF, which were primarily designed to act as antimicrobial agents as well as neutralizers of bacterial endotoxin (lipopolysaccharide, LPS), Here, two selected peptides, a 17- and a 19-mer, were characterized physicochemically and in biological test systems. The secondary structure of the peptides indicates essentially a ?-sheet including antiparallel strands, the latter being reduced when the peptides bind to LPS. A very strong exothermic binding due to attractive Coulomb interactions governs the LPS-peptide reaction, which additionally leads to a fluidization of the acyl chains of LPS. A comparison of the interaction of the peptide with negatively charged phosphatidylserine shows in contrast a rigidification of the acyl chains of the lipid. Finally, the biological assays reveal a diverging behaviour of the two peptides, with higher antibacterial activity of the 17-mer, but a much higher activity of the 19-mer in its ability to inhibit the LPS-induced cytokine production in human mononuclear cells.
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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/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Arthropod Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Invertebrate Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/antilipopolysaccharide factor...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1875-5305
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1328-33
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:20673224-Amino Acid Sequence,
pubmed-meshheading:20673224-Antimicrobial Cationic Peptides,
pubmed-meshheading:20673224-Arthropod Proteins,
pubmed-meshheading:20673224-Calorimetry,
pubmed-meshheading:20673224-Cells, Cultured,
pubmed-meshheading:20673224-Humans,
pubmed-meshheading:20673224-Invertebrate Hormones,
pubmed-meshheading:20673224-Leukocytes, Mononuclear,
pubmed-meshheading:20673224-Lipids,
pubmed-meshheading:20673224-Lipopolysaccharides,
pubmed-meshheading:20673224-Molecular Sequence Data,
pubmed-meshheading:20673224-Phase Transition,
pubmed-meshheading:20673224-Protein Structure, Secondary,
pubmed-meshheading:20673224-Tumor Necrosis Factor-alpha
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pubmed:year |
2010
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pubmed:articleTitle |
Physicochemical and biological characterization of anti-endotoxin peptides and their influence on lipid properties.
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pubmed:affiliation |
Forschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, D-23845 Borstel, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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