Source:http://linkedlifedata.com/resource/pubmed/id/12097167
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2002-7-4
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| pubmed:abstractText |
We previously showed that bovine apolipoprotein A-II (apoA-II) has antimicrobial activity against Escherichia coli in PBS, and its C-terminal residues 49-76 are responsible for the activity using synthetic peptides. In order to understand the structural requirements of peptide 49-76 for the antimicrobial activity, the N- or C-terminus was truncated and then the charged (Lys or Asp) or Ser residues were replaced by Ala. Deletion of the first or last three amino acids and replacement of Lys-54/55 or 71/72 by Ala caused a substantial decreases in alpha-helical content in 50% TFE, showing the possible presence of helices in N- and C-terminal regions, respectively. The anti-Escherichia coli activity of the peptide correlated with its liposome-binding activity. Replacement of Lys-54/55 or 71/72 by Ala resulted in an almost complete loss of anti-E. coli activity with a substantial decrease in liposome-binding activity. Moreover, deletion of the last three amino acids caused a reduction to 1/17 of the original anti-E. coli activity with a moderate decrease in liposome-binding activity. In contrast, replacement of Ser-65/66, Asp-59, or Asp-69 by Ala hardly affected the anti-E. coli activity. These findings suggest that Lys-54/55 and Lys-71/72 on the putative helices are critical for antimicrobial activity, and the C-terminal 3 amino acids are important for the structural integrity of the C-terminal region for effective antimicrobial activity.
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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 |
Jul
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| pubmed:issn |
0021-924X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
132
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
115-9
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| pubmed:dateRevised |
2007-12-19
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| pubmed:meshHeading |
pubmed-meshheading:12097167-Amino Acid Sequence,
pubmed-meshheading:12097167-Amino Acid Substitution,
pubmed-meshheading:12097167-Animals,
pubmed-meshheading:12097167-Anti-Bacterial Agents,
pubmed-meshheading:12097167-Apolipoprotein A-II,
pubmed-meshheading:12097167-Cattle,
pubmed-meshheading:12097167-Circular Dichroism,
pubmed-meshheading:12097167-Escherichia coli,
pubmed-meshheading:12097167-Inhibitory Concentration 50,
pubmed-meshheading:12097167-Liposomes,
pubmed-meshheading:12097167-Microbial Sensitivity Tests,
pubmed-meshheading:12097167-Microscopy, Electron,
pubmed-meshheading:12097167-Molecular Sequence Data,
pubmed-meshheading:12097167-Peptides,
pubmed-meshheading:12097167-Protein Binding,
pubmed-meshheading:12097167-Protein Structure, Secondary,
pubmed-meshheading:12097167-Structure-Activity Relationship
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| pubmed:year |
2002
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| pubmed:articleTitle |
Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II.
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| pubmed:affiliation |
Department of Biochemistry Yamanashi Medical University, Nakakoma, Yamanashi 409-3898, Japan. mitsum@swallow.res.yamanashi-med.ac.jp
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| pubmed:publicationType |
Journal Article
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