Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides

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dc.contributor.authorSong Yub Shin-
dc.contributor.authorJoo Hyun Kang-
dc.contributor.authorKyung Soo Hahm-
dc.date.accessioned2017-04-19T08:56:08Z-
dc.date.available2017-04-19T08:56:08Z-
dc.date.issued1999-
dc.identifier.issn1397-002X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4750-
dc.description.abstractIn 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.publisherWiley-
dc.titleStructure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides-
dc.title.alternativeStructure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides-
dc.typeArticle-
dc.citation.titleChemical Biology & Drug Design-
dc.citation.number0-
dc.citation.endPage90-
dc.citation.startPage82-
dc.citation.volume53-
dc.contributor.affiliatedAuthorSong Yub Shin-
dc.contributor.affiliatedAuthorJoo Hyun Kang-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName강주현-
dc.contributor.alternativeName함경수-
dc.identifier.bibliographicCitationChemical Biology & Drug Design, vol. 53, pp. 82-90-
dc.identifier.doi10.1111/j.1399-3011.1999.tb01620.x-
dc.subject.keywordantibacterial activity-
dc.subject.keywordantitumor activity-
dc.subject.keywordhemolytic activity-
dc.subject.keywordhybrid peptides-
dc.subject.localAntibacterial activity-
dc.subject.localantibacterial activity-
dc.subject.localAntitumor activity-
dc.subject.localanti-tumor activity-
dc.subject.localantitumor activity-
dc.subject.localHemolytic activity-
dc.subject.localhemolytic activity-
dc.subject.localhybrid peptides-
dc.description.journalClassY-
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