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C-terminal amidation of PMAP-23: translocation to the inner membrane of Gram-negative bacteria

Title
C-terminal amidation of PMAP-23: translocation to the inner membrane of Gram-negative bacteria
Author
윤문영
Keywords
PMAP-23; Antimicrobial peptide; Lipopolysaccharide; Amidation; Translocation; Membrane bilayer
Issue Date
2011-01
Publisher
SPRINGER
Citation
AMINO ACIDS, v. 40, NO 1, Page. 183-195
Abstract
PMAP-23 is a member of the cathelicidin family derived from pig myeloid cells and has potent antimicrobial activity. Amidation of the carboxyl terminus (C-terminus) of an antimicrobial peptide generally enhances its structural stability and antimicrobial activity or decreases its cytotoxicity. The aim of the present study was to investigate the effect of amidation on the mode of action in PMAP-23. Irrespective of amidation, PMAP-23 adopts a helix-hinge-helix structure in a membrane-mimetic environment. The antibacterial activities of PMAP-23C, which had a free C-terminus, and PMAP-23N, which had an amidated C-terminus, were similar against Gram-negative bacteria, reflecting a similar ability to neutralize lipopolysaccharide. However, PMAP-23N assumed a perpendicular orientation across the outer to the inner leaflet of the bacterial inner membrane, while PMAP-23C was orientated parallel to the lipid bilayer, as determined by following the blue shift in tryptophan fluorescence, as well as calcein release from liposomes and SYTOX Green uptake assays. These results suggest that N-terminal amidation of PMAP-23 provides structural stability and increases the peptide's cationic charge, facilitating translocation into the bacterial inner membrane.
URI
https://link.springer.com/article/10.1007%2Fs00726-010-0632-1
ISSN
0939-4451; 1438-2199
DOI
10.1007/s00726-010-0632-1
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > CHEMISTRY(화학과) > Articles
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