Skip Navigation


Journal of Biochemistry Advance Access originally published online on April 19, 2008
Journal of Biochemistry 2008 144(2):167-176; doi:10.1093/jb/mvn056
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
144/2/167    most recent
mvn056v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yoshida, N.
Right arrow Articles by Onda, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshida, N.
Right arrow Articles by Onda, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Japanese Biochemical Society

Susceptibilities of Phospholipid Membranes Containing Cholesterol or Ergosterol to Gramicidin and its Derivative Incorporated in Lysophospholipid Micelles

Naoko Yoshida1, Tomoyoshi Mita2 and Maki Onda2,*

1Department of Environmental Sciences, Faculty of Science, Osaka Women's University; and 2Department of Biological Science, Graduate School of Science, Osaka Prefecture University, Japan

*To whom correspondence should be addressed. Tel: and Fax: +81-72-254-9185, E-mail: onda{at}b.s.osakafu-u.ac.jp

Received March 29, 2008; Accepted April 8, 2008


   Abstract

Complex formation of gramicidin (GA) and desformylgramicidin (des-GA) with sterols was investigated by measuring the intrinsic Trp fluorescence. In organic solvents, the Trp fluorescence of momeric GA was quenched upon binding either cholesterol or ergosterol, but that of monomeric des-GA was not quenched by adding cholesterol. Both dimeric GA and des-GA bound highly to ergosterol, but not to cholesterol, determined by quenching of Trp fluorescence. Furthermore, GA- and des-GA-loaded lysophosphatidylcholine micelles were incubated with phosphatidylcholine vesicles containing cholesterol or ergosterol. The results showed that both monomeric and dimeric peptides hardly bound to cholesterol incorporated into phospholipid vesicles, but markedly bound to ergosterol incorporated into the bilayer membranes. Interestingly, des-GA bound more specifically to the two sterols than GA. In addition, fluorescence resonance energy transfer analysis showed that des-GA bound more specifically to the two sterol than GA.

Key Words: drug delivery systems, fluorescence, gramicidin, Lysophospholipid, sterol

Abbreviations: CMC, critical micelle concentration; des-GA, desformylgramicidin; DMSO, dimethyl sulphoxide; DPPC, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine; eggPC, egg-yolk phosphatidylcholine; FRET, fluorescence resonance energy transfer; GA, gramicidin; LPC, lysophosphatidylcholine; NATA, N-acetyltryptophanamide; THF, tetrahydrofuran; TNS, 2-(p-toluidino)naphthalene-6-sulphonic acid


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.