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Title 

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

Authors 

Seung-Wook ChiJ S KimDo-Heyoung KimSi Hyung LeeY H ParkKyou Hoon Han

Publisher 

Elsevier

Issue Date 

2007

Citation 

Biochemical and Biophysical Research Communications, vol. 352, no. 3, pp. 592-597

Keywords 

anti-infective peptidegaegurin 4hemolysisNMRsolution structurepolypeptide antibiotic agentcell interactioncell membranechemical interactionchemical structure

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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2006.11.064

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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