Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 윤문영 | - |
dc.date.accessioned | 2018-02-02T04:53:03Z | - |
dc.date.available | 2018-02-02T04:53:03Z | - |
dc.date.issued | 2011-01 | - |
dc.identifier.citation | AMINO ACIDS, v. 40, NO 1, Page. 183-195 | en_US |
dc.identifier.issn | 0939-4451 | - |
dc.identifier.issn | 1438-2199 | - |
dc.identifier.uri | https://link.springer.com/article/10.1007%2Fs00726-010-0632-1 | - |
dc.description.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. | en_US |
dc.description.sponsorship | This work was supported by the Pioneer Research Program for Converging Technology of the Ministry of Education, Science and Technology, Republic of Korea (Grant No. 20100002201) and research funds from Chosun University in 2008. | en_US |
dc.language.iso | en | en_US |
dc.publisher | SPRINGER | en_US |
dc.subject | PMAP-23 | en_US |
dc.subject | Antimicrobial peptide | en_US |
dc.subject | Lipopolysaccharide | en_US |
dc.subject | Amidation | en_US |
dc.subject | Translocation | en_US |
dc.subject | Membrane bilayer | en_US |
dc.title | C-terminal amidation of PMAP-23: translocation to the inner membrane of Gram-negative bacteria | en_US |
dc.type | Article | en_US |
dc.relation.no | 1 | - |
dc.relation.volume | 40 | - |
dc.identifier.doi | 10.1007/s00726-010-0632-1 | - |
dc.relation.page | 183-195 | - |
dc.relation.journal | AMINO ACIDS | - |
dc.contributor.googleauthor | Kim, Jin-Young | - |
dc.contributor.googleauthor | Park, Seong-Cheol | - |
dc.contributor.googleauthor | Yoon, Moon-Young | - |
dc.contributor.googleauthor | Hahm, Kyung-Soo | - |
dc.contributor.googleauthor | Park, Yoonkyung | - |
dc.relation.code | 2011200575 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF NATURAL SCIENCES[S] | - |
dc.sector.department | DEPARTMENT OF CHEMISTRY | - |
dc.identifier.pid | myyoon | - |
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