2010年5月
Metal-Assisted Channel Stabilization: Disposition of a Single Histidine on the N-terminus of Alamethicin Yields Channels with Extraordinarily Long Lifetimes
BIOPHYSICAL JOURNAL
- ,
- ,
- 巻
- 98
- 号
- 9
- 開始ページ
- 1801
- 終了ページ
- 1808
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bpj.2010.01.028
- 出版者・発行元
- CELL PRESS
Alamethicin, a member of the peptaibol family of antibiotics, is a typical channel-forming peptide with a helical structure. The self-assembly of the peptide in the membranes yields voltage-dependent channels. In this study, three alamethicin analogs possessing a charged residue (His, Lys, or Glu) on their N-termini were designed with the expectation of stabilizing the transmembrane structure. A slight elongation of channel lifetime was observed for the Lys and Glu analogs. On the other hand, extensive stabilization of certain channel open states was observed for the His analog. This stabilization was predominantly observed in the presence of metal ions such as Zn(2+), suggesting that metal coordination with His facilitates the formation of a supramolecular assembly in the membranes. Channel stability was greatly diminished by acetylation of the N-terminal amino group, indicating that the N-terminal amino group also plays an important role in metal coordination.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.bpj.2010.01.028
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201102209060689209
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/20441743
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000277377300013&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1016/j.bpj.2010.01.028
- ISSN : 0006-3495
- J-Global ID : 201102209060689209
- PubMed ID : 20441743
- Web of Science ID : WOS:000277377300013