Antibacterial, antitumor and hemolytic activities of α-helical antibiotic peptide, P₁8 and its analogs

Cited 91 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorS Y Shin-
dc.contributor.authorS H Lee-
dc.contributor.authorS T Yang-
dc.contributor.authorE J Park-
dc.contributor.authorD G Lee-
dc.contributor.authorMyung Kyu Lee-
dc.contributor.authorS H Eom-
dc.contributor.authorW K Song-
dc.contributor.authorY Kim-
dc.contributor.authorKyung Soo Hahm-
dc.contributor.authorJ I Kim-
dc.date.accessioned2017-04-19T08:58:57Z-
dc.date.available2017-04-19T08:58:57Z-
dc.date.issued2001-
dc.identifier.issn1397002X-
dc.identifier.uri10.1034/j.1399-3011.2001.00934.xko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5801-
dc.description.abstractThe α-helical antibiotic peptide (P18: KWKLFKKIPKFLHLAKKF-NH2) designed from the cecropin A(1-8)-magainin 2 (1-12) hybrid displayed strong bactericidal and tumoricidal activity without in ducing hemolysis. The effect of the Pro9 residue at central position of P18 on cell selectivity was investigated by Pro9 → Leu or Pro9 → Ser substitution. Either substitution markedly reduced the antibacterial activity of P18 and increased hemolysis, although it did not significantly affect cytotoxicity against human transformed tumor and normal fibroblast cells. These results suggest that a proline kink in α-helical antibiotic peptide P18 serves as a hinge region to facilitate ion channel formation on bacterial cell membranes and thus plays an important role in providing high selectivity against bacterial cells. Furthermore, to investigate the structure-antibiotic activity relationships of P18, a series of N- or C-terminal deletion and substitution analogs of P18 were synthesized. The C-terminal region of P18 was related to its antibiotic activity and α-helical conformation on lipid membranes rather than N-terminal one. Higher α-helicity of the peptides was involved in the hemolytic and antitumor activity rather than antibacterial activity. Except for [L9]-P18 and [S9]-P18, all the designed peptides containing a Pro residue showed potent antibacterial activity, although they did not induce a cytolytic effect against human erythrocyte and normal fibroblast cells at the concentration required to kill bacteria. In particular, P18 and some analogs (N-1, N-2, N-3, N-3L and N-4L) with potent bactericidal and tumoricidal activity and little or no normal cell toxicity may serve as an attractive candidate for the development of novel anti-infective or antitumor agents.-
dc.publisherWiley-
dc.titleAntibacterial, antitumor and hemolytic activities of α-helical antibiotic peptide, P₁8 and its analogs-
dc.title.alternativeAntibacterial, antitumor and hemolytic activities of α-helical antibiotic peptide, P₁8 and its analogs-
dc.typeArticle-
dc.citation.titleChemical Biology & Drug Design-
dc.citation.number6-
dc.citation.endPage514-
dc.citation.startPage504-
dc.citation.volume58-
dc.contributor.affiliatedAuthorMyung Kyu Lee-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName이시형-
dc.contributor.alternativeName양성택-
dc.contributor.alternativeName-
dc.contributor.alternativeName이동건-
dc.contributor.alternativeName이명규-
dc.contributor.alternativeName엄수한-
dc.contributor.alternativeName-
dc.contributor.alternativeName김양미-
dc.contributor.alternativeName함경수-
dc.contributor.alternativeName김재일-
dc.identifier.bibliographicCitationChemical Biology & Drug Design, vol. 58, no. 6, pp. 504-514-
dc.identifier.doi10.1034/j.1399-3011.2001.00934.x-
dc.subject.keywordα-helical antibiotic peptide-
dc.subject.keywordantibiotic activity-
dc.subject.keywordcell selectivity-
dc.subject.keywordP18-
dc.subject.keywordPro kink-
dc.subject.localα-helical antibiotic peptide-
dc.subject.localantibiotic activity-
dc.subject.localAntibiotic activity-
dc.subject.localcell selectivity-
dc.subject.localP18-
dc.subject.localPro kink-
dc.description.journalClassY-
Appears in Collections:
Division of Biomaterials Research > Bionanotechnology Research Center > 1. 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.