DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kobayashi, S | ko |
dc.contributor.author | Takeshima, K | ko |
dc.contributor.author | Park, CB | ko |
dc.contributor.author | Kim, Sun-Chang | ko |
dc.contributor.author | Matsuzaki, K | ko |
dc.date.accessioned | 2013-03-02T17:55:08Z | - |
dc.date.available | 2013-03-02T17:55:08Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-07 | - |
dc.identifier.citation | BIOCHEMISTRY, v.39, no.29, pp.8648 - 8654 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10203/74806 | - |
dc.description.abstract | Buforin 2 is an antimicrobial peptide discovered in the stomach tissue of the Asian toad Bufo bufo gargarizans. The 21-residue peptide with +6 net charge shows antimicrobial activity an order of magnitude higher than that of magainin 2, a membrane-permeabilizing antimicrobial peptide from Xenopus laevis [Park, C. B., Kim, M. S., and Kim, S. C. (1996) Biochem. Biophys. Res. Commun. 218, 408-413]. In this study, we investigated the interactions of buforin 2 with phospholipid bilayers in comparison with magainin 2 to obtain insight into the mechanism of action of buforin 2. Equipotent Trp-substituted peptides were used to fluorometrically monitor peptide-lipid interactions. Circular dichroism measurements showed that buforin 2 selectively bound to liposomes composed of acidic phospholipids, assuming a secondary structure similar to that in trifluoroethanol/water, which is an amphipathic helix distorted around Pro(11) with a flexible N-terminal region [Yi, G. S., Park, C. B., Kim, S. C., and Cheong, C. (1996) FEES Lett. 398, 87-90]. Magainin 2 induced the leakage of a fluorescent dye entrapped within lipid vesicles coupled to Lipid flip-flop. These results have been interpreted as the formation of a peptide-lipid supramolecular complex pore [Matsuzaki, K. (1998) Biochim. Biophys. Acta 1376, 391-400]. Buforin 2 exhibited much weaker membrane permeabilization activity despite its higher antimicrobial activity. In contrast, buforin 2 was more efficiently translocated across lipid bilayers than magainin 2. These results suggested that the ultimate target of buforin 2 is not the membrane but intracellular components. Furthermore, buforin 2 induced no lipid flip-flop, indicating that the mechanism of translocation of buforin 2 is different from that of magainin 2. The role of Pro was investigated by use of a P11A derivative of buforin 2. The derivation caused a change to magainin 2-like secondary structure and membrane behavior. Pro(11) was found to be a very important structural factor for the unique properties of buforin 2. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | ANTIBACTERIAL PEPTIDES | - |
dc.subject | PHOSPHOLIPID-BILAYERS | - |
dc.subject | PORE FORMATION | - |
dc.subject | HISTONE H2A | - |
dc.subject | MAGAININ-2 | - |
dc.subject | MEMBRANE | - |
dc.subject | MECHANISM | - |
dc.subject | ALAMETHICIN | - |
dc.subject | ANALOGS | - |
dc.title | Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor | - |
dc.type | Article | - |
dc.identifier.wosid | 000088376900034 | - |
dc.identifier.scopusid | 2-s2.0-0034713613 | - |
dc.type.rims | ART | - |
dc.citation.volume | 39 | - |
dc.citation.issue | 29 | - |
dc.citation.beginningpage | 8648 | - |
dc.citation.endingpage | 8654 | - |
dc.citation.publicationname | BIOCHEMISTRY | - |
dc.contributor.localauthor | Kim, Sun-Chang | - |
dc.contributor.nonIdAuthor | Kobayashi, S | - |
dc.contributor.nonIdAuthor | Takeshima, K | - |
dc.contributor.nonIdAuthor | Park, CB | - |
dc.contributor.nonIdAuthor | Matsuzaki, K | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ANTIBACTERIAL PEPTIDES | - |
dc.subject.keywordPlus | PHOSPHOLIPID-BILAYERS | - |
dc.subject.keywordPlus | PORE FORMATION | - |
dc.subject.keywordPlus | HISTONE H2A | - |
dc.subject.keywordPlus | MAGAININ-2 | - |
dc.subject.keywordPlus | MEMBRANE | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | ALAMETHICIN | - |
dc.subject.keywordPlus | ANALOGS | - |
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