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Title 

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

Authors 

Joo Hyun KangSong Yub ShinSo Yun JangKil Lyong KimKyung Soo Hahm

Publisher 

Elsevier

Issue Date 

1999

Citation 

Biochemical and Biophysical Research Communications, vol. 264, no. 0, pp. 281-286

Keywords 

antibiotic agentpeptidetryptophanantibacterial activityantimicrobial cationic peptidespeptide biosynthesispeptides

Abstract 

PMAP-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.

ISSN 

0006-291X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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