DC Field | Value | Language |
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dc.contributor.author | Song Yub Shin | - |
dc.contributor.author | Joo Hyun Kang | - |
dc.contributor.author | Kyung Soo Hahm | - |
dc.date.accessioned | 2017-04-19T08:56:08Z | - |
dc.date.available | 2017-04-19T08:56:08Z | - |
dc.date.issued | 1999 | - |
dc.identifier.issn | 1397-002X | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/4750 | - |
dc.description.abstract | In order to elucidate the structure-antibiotic activity relationship of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides, several truncated peptides and the analogues with amino acid substitutions were synthesized and their antibacterial, antitumor and hemolytic activities of were examined. Cecropin A-magainin 2 hybrid analog, L16-CA(1-8)-MA(1-12) (termed as L-CA-MA in this study: KWKLFKKIGIGKFLHLAKKF-NH2), is known to have potent antibacterial and antitumor activity with less hemolytic activity. We found that the C-terminal region of L-CA-MA is more involved in the α-helical structure on cell membrane-like environment than N-terminal one by circular dichroism analysis. Deletion of the Gly-Ile-Gly sequence, the central hinge region of L-CA-MA, produced a considerable reduction in antitumor and hemolytic activity rather than an antibacterial one. The insertion of Pro, Gly-Ile or Gly-Pro in this hinge region of L-CA-MA caused retention of both antibacterial and antitumor activity while causing a significant decrease in hemolytic activity. However, the substitution with Gly-Pro-Gly instead of the Gly-Ile-Gly in CA(1-8)-MA(1-12), CA(1-8)-ME(1- 12), CA(1-13)-MA(1-13) and CA(1-13)-ME(1-13) hybrids resulted in a drastic decrease in antibacterial, antitumor and hemolytic activity. The increase of hydrophobicity at position 16 in CA(1-8)-MA(1-12) by substituting Trp or Phe induced a significant increase in hemolytic activity without a considerable change in either antibacterial or antitumor activity. Therefore, these results suggested that the appropriate flexibility in the hinge region of CA- MA and CA-ME hybrid peptides and the appropriate hydrophobicity at position 16 in the hydrophobic region of CA (1-8)-MA(1-12) are important in potent antibacterial and antitumor activity with no hemolytic effect. | - |
dc.publisher | Wiley | - |
dc.title | Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides | - |
dc.title.alternative | Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides | - |
dc.type | Article | - |
dc.citation.title | Chemical Biology & Drug Design | - |
dc.citation.number | 0 | - |
dc.citation.endPage | 90 | - |
dc.citation.startPage | 82 | - |
dc.citation.volume | 53 | - |
dc.contributor.affiliatedAuthor | Song Yub Shin | - |
dc.contributor.affiliatedAuthor | Joo Hyun Kang | - |
dc.contributor.affiliatedAuthor | Kyung Soo Hahm | - |
dc.contributor.alternativeName | 신송엽 | - |
dc.contributor.alternativeName | 강주현 | - |
dc.contributor.alternativeName | 함경수 | - |
dc.identifier.bibliographicCitation | Chemical Biology & Drug Design, vol. 53, pp. 82-90 | - |
dc.identifier.doi | 10.1111/j.1399-3011.1999.tb01620.x | - |
dc.subject.keyword | antibacterial activity | - |
dc.subject.keyword | antitumor activity | - |
dc.subject.keyword | hemolytic activity | - |
dc.subject.keyword | hybrid peptides | - |
dc.subject.local | Antibacterial activity | - |
dc.subject.local | antibacterial activity | - |
dc.subject.local | Antitumor activity | - |
dc.subject.local | anti-tumor activity | - |
dc.subject.local | antitumor activity | - |
dc.subject.local | Hemolytic activity | - |
dc.subject.local | hemolytic activity | - |
dc.subject.local | hybrid peptides | - |
dc.description.journalClass | Y | - |
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