Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4

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Title
Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4
Author(s)
Seung-Wook Chi; J S Kim; Do-Heyoung Kim; Si Hyung Lee; Y H Park; Kyou Hoon Han
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 352, no. 3, pp. 592-597
Publication Year
2007
Abstract
We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.
Keyword
anti-infective peptidegaegurin 4hemolysisNMRsolution structure
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2006.11.064
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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