| pubmed-article:10432319 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10432319 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:10432319 | lifeskim:mentions | umls-concept:C0085202 | lld:lifeskim |
| pubmed-article:10432319 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:10432319 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:10432319 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:10432319 | pubmed:dateCreated | 1999-10-20 | lld:pubmed |
| pubmed-article:10432319 | pubmed:abstractText | We previously showed that bovine apolipoprotein A-II (apoA-II) had antimicrobial activity against Escherichia coli and the yeast Saccharomyces cerevisiae in PBS. We have characterized here the active domain of apoA-II using synthetic peptides. A peptide corresponding to C-terminal residues Leu(49)-Thr(76) exhibited significant antimicrobial activity against E. coli in PBS, but not against S. cerevisiae. Experiments using amino-acid-substituted peptides indicated that the residues Phe(52)-Phe(53)-Lys(54)-Lys(55) are required for the activity. Peptide Leu(49)-Thr(76) induced the release of calcein trapped inside the vesicles whose lipid composition resembles that of E. coli membrane, suggesting that peptide Leu(49)-Thr(76) can destabilize the E. coli membrane. CD measurements showed that the alpha-helicity of peptide Leu(49)-Thr(76) increased from 3.5 to 36% by addition of the vesicles. When E. coli cells were incubated with peptide Leu(49)-Thr(76), some proteins were released to the external medium, probably owing to membrane destabilization caused by the peptide. In electron micrographs of E. coli cells treated with peptide Leu(49)-Thr(76), transparent nucleoids and granulated cytoplasm were observed. Amino acid substitutions, Phe(52)Phe(53)-->AlaAla (Phe(52, 53)-->Ala) in peptide Leu(49)-Thr(76) caused the loss of antimicrobial activity against E. coli, although protein-releasing activity was retained. Electron micrographs of the cells treated with peptide Leu(49)-Thr(76)(Phe(52,53)-->Ala) revealed morphological change only at the nucleoids. Therefore peptide Leu(49)-Thr(76) appears to primarily target the cytoplasm rather than the membrane of E. coli cells. | lld:pubmed |
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| pubmed-article:10432319 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10432319 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10432319 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10432319 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10432319 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10432319 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10432319 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:SamejimaTT | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:YamadaMM | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:LUNTM RMR | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:SatohTT | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:YokotaSS | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:ShimamuraSS | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:TsurugiKK | lld:pubmed |
| pubmed-article:10432319 | pubmed:author | pubmed-author:MotizukiMM | lld:pubmed |
| pubmed-article:10432319 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10432319 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10432319 | pubmed:volume | 342 ( Pt 1) | lld:pubmed |
| pubmed-article:10432319 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10432319 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10432319 | pubmed:pagination | 215-21 | lld:pubmed |
| pubmed-article:10432319 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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