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A Helix-induced Oligomeric Transition of Gaegurin 4, an Antimicrobial Peptide Isolated from a Korean Frog
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Eun, Su-Yong | - |
dc.contributor.author | Jang, Hae-Kyung | - |
dc.contributor.author | Han, Seong-Kyu | - |
dc.contributor.author | Ryu, Pan Dong | - |
dc.contributor.author | Lee, Byeong Jae | - |
dc.contributor.author | Han, Kyou-Hoon | - |
dc.contributor.author | Kim, Soon-Jong | - |
dc.date.accessioned | 2009-08-07T03:22:18Z | - |
dc.date.available | 2009-08-07T03:22:18Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Mol. Cells. 21, 229-236 | en |
dc.identifier.issn | 1016-8478 (print) | - |
dc.identifier.issn | 0219-1032 (online) | - |
dc.identifier.uri | http://molcells.inforang.com/about/journal_view.html?uid=415 | - |
dc.identifier.uri | https://hdl.handle.net/10371/6487 | - |
dc.description.abstract | Gaegurin 4 (GGN4), a novel peptide isolated from the skin of a Korean frog, Rana rugosa, has broad spectrum antimicrobial activity. A number of amphipathic peptides closely related to GGN4 undergo a coil to helix transition with concomitant oligomerization in lipid membranes or membrane-mimicking environments. Despite intensive study of their secondary structures, the oligomeric states of the peptides before and after the transition are not well understood. To clarify the structural basis of its antibiotic action, we used analytical ultracentrifugation to define the aggregation state of GGN4 in water, ethyl alcohol, and 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP). The maximum size of GGN4 in 15% HFIP corresponded to a decamer, whereas it was monomeric in buffer. The oligomeric transition is accompanied by a cooperative 9 nm blue-shift of maximum fluorescence emission and a large secondary structure change from an almost random coil to an alpha-helical structure. GGN4 induces pores in lipid membranes and, using electrophysiological methods, we estimated the diameter of the pores to be exceed 7.3 A, which suggests that the minimal oligomer structure responsible is a pentamer. | en |
dc.description.sponsorship | This study was supported by a grant from
the Biomedical Brain Research Center of the Korea, Health 21 R&D Project, funded by the Ministry of Health & Welfare, Republic of Korea (A040042), to S.-Y. Eun, and an intramural grant from Mokpo National University to S.-J. Kim. | en |
dc.language.iso | en | - |
dc.publisher | 한국분자·세포생물학회 = Korean Society of Molecular and Cellular Biology | en |
dc.subject | Aggregation State | en |
dc.subject | Analytical Ultracentrifuge | en |
dc.subject | Antimicrobial Peptide | en |
dc.subject | Gaegurin 4 | en |
dc.title | A Helix-induced Oligomeric Transition of Gaegurin 4, an Antimicrobial Peptide Isolated from a Korean Frog | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 은수용 | - |
dc.contributor.AlternativeAuthor | 장혜경 | - |
dc.contributor.AlternativeAuthor | 한성규 | - |
dc.contributor.AlternativeAuthor | 류판동 | - |
dc.contributor.AlternativeAuthor | 이병재 | - |
dc.contributor.AlternativeAuthor | 한규훈 | - |
dc.contributor.AlternativeAuthor | 김순종 | - |
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