| Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: proline as a translocation promoting factor. | |
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MedLine Citation:
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PMID: 10913273 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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) FEBS 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. |
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Authors:
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S Kobayashi; K Takeshima; C B Park; S C Kim; K Matsuzaki |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry Volume: 39 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 2000 Jul |
Date Detail:
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Created Date: 2000-08-15 Completed Date: 2000-08-15 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 8648-54 Citation Subset: IM |
Affiliation:
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Graduate Schools of Pharmaceutical Sciences and Biostudies, Kyoto University, Japan. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Anti-Bacterial Agents / chemistry*, pharmacology* Antimicrobial Cationic Peptides* Binding Sites Biological Transport, Active / drug effects Bufo bufo Circular Dichroism Diffusion Escherichia coli / drug effects Humans Lipid Bilayers / chemistry* Molecular Sequence Data Peptides / chemistry, pharmacology Permeability Proline / chemistry Proteins / chemistry*, pharmacology* Xenopus Proteins* |
| Chemical | |
Reg. No./Substance:
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0/Anti-Bacterial Agents; 0/Antimicrobial Cationic Peptides; 0/Lipid Bilayers; 0/Peptides; 0/Proteins; 0/Xenopus Proteins; 0/buforin II; 108433-95-0/magainin 2 peptide, Xenopus; 147-85-3/Proline |
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