Effects of tryptophan residues of porcine myeloid antibacterial peptide PMAP-23 on antibiotic activity

Cited 21 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorJoo Hyun Kang-
dc.contributor.authorSong Yub Shin-
dc.contributor.authorSo Yun Jang-
dc.contributor.authorKil Lyong Kim-
dc.contributor.authorKyung Soo Hahm-
dc.date.accessioned2017-04-19T08:56:25Z-
dc.date.available2017-04-19T08:56:25Z-
dc.date.issued1999-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4840-
dc.description.abstractPMAP-23 is a 23-residue antimicrobial peptide from porcine myeloid cells. In order to determine the effects of two Trp residues in positions 7 and 21 of PMAP-23 on antibacterial activity and phospholipid vesicle interacting property, two analogues in which Ala is substituted for Trp residue in position 7 or 21 were synthesized. A21-PMAP-23 exhibited reduced antibacterial activity and phospholipid vesicle disrupting activity when compared to those of PMAP-23 and A7-PMAP-23. PMAP-23 readily interacted with model lipid membrane and induced membrane destabilization. Therefore antibacterial activity induced by PMAP-23 is due to the interaction of cell membrane with peptide followed by membrane perturbation. A significant structural change on the SDS micelle was not found by Ala substitution of the Trp residue of PMAP-23. Also, there is a good correlation between hydrophobic interaction on RP-HPLC, expressed as retention time on RP-HPLC, and antibacterial activity. The vesicle titration experiment indicated that Trp residues located at near C-terminus are accessible to hydrophobic tail of phospholipid vesicle. This result suggests that the C-terminal end of PMAP-23 penetrates into the lipid bilayer in the course of the interaction with phospholipid membranes and is important for its antibacterial activity.-
dc.publisherElsevier-
dc.titleEffects of tryptophan residues of porcine myeloid antibacterial peptide PMAP-23 on antibiotic activity-
dc.title.alternativeEffects of tryptophan residues of porcine myeloid antibacterial peptide PMAP-23 on antibiotic activity-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number0-
dc.citation.endPage286-
dc.citation.startPage281-
dc.citation.volume264-
dc.contributor.affiliatedAuthorKil Lyong Kim-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.alternativeName강주현-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName장소윤-
dc.contributor.alternativeName김길룡-
dc.contributor.alternativeName함경수-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 264, pp. 281-286-
dc.identifier.doi10.1006/bbrc.1999.1510-
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.