Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides

Cited 0 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorSong Yub Shin-
dc.contributor.authorMyung Kyu Lee-
dc.contributor.authorKil Lyong Kim-
dc.contributor.authorKyung Soo Hahm-
dc.date.accessioned2017-04-19T08:54:50Z-
dc.date.available2017-04-19T08:54:50Z-
dc.date.issued1997-
dc.identifier.issn1397-002X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4199-
dc.description.abstractThe hybrid peptide (CA-ME) derived from cecropin A(1-8) and melittin(1- 12) has potent antibacterial and antimalarial activities. Because the N- terminal sequence 1-12 of magainin 2 is similar to melittin(1-12), CA-MA with CA(1-8) and MA(1-12) and their analogues were designed and synthesized. Antitumor activities of these peptides were evaluated using three small cell lung cancer cell lines. Greater antitumor activity was observed when the residues 16, 18 and 19 of the peptide were hydrophobic (Leu or Val), basic (Lys) and basic (Lys), respectively. The IC50 values of the peptides with the residues were 2 to 4 μM. Residue 12 was related to hemolytic activity rather than antitumor activity. Increase in amphipathicity of P4 enhanced hemolytic activity without significant change in antitumor activity. The α- helicity of the peptides in a 30 nm sodium dodecyl sulfate solution was more closely correlated to hemolytic activity than antitumor activity.-
dc.publisherWiley-
dc.titleStructure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides-
dc.title.alternativeStructure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides-
dc.typeArticle-
dc.citation.titleChemical Biology & Drug Design-
dc.citation.number0-
dc.citation.endPage285-
dc.citation.startPage279-
dc.citation.volume50-
dc.contributor.affiliatedAuthorSong Yub Shin-
dc.contributor.affiliatedAuthorMyung Kyu Lee-
dc.contributor.affiliatedAuthorKil Lyong Kim-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName이명규-
dc.contributor.alternativeName김길룡-
dc.contributor.alternativeName함경수-
dc.identifier.bibliographicCitationChemical Biology & Drug Design, vol. 50, pp. 279-285-
dc.subject.keywordHybrid peptides-
dc.subject.keywordantitumor activity-
dc.subject.keywordhemolytic activity-
dc.subject.keywordα-helicity-
dc.subject.localHybrid peptide-
dc.subject.localHybrid peptides-
dc.subject.localhybrid peptide-
dc.subject.localanti-tumor activity-
dc.subject.localantitumor activity-
dc.subject.localAntitumor activity-
dc.subject.localHemolytic activity-
dc.subject.localhemolytic activity-
dc.subject.localα-helicity-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.