Issue 4, 2006
From the journal:

Chemical Communications

Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles

Riccardo Ferdani,a   Robert Pajewski,a   Jolanta Pajewska,a   Paul H. Schlesingerb  and  George W. Gokel*ac  

* Corresponding authors

a Department of Molecular Biology & Pharmacology, Washington University School of Medicine, 660 S. Euclid Avenue, Box 8103, St. Louis, USA

b Department of Molecular Cell Biology, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, USA

c Department of Chemistry, Washington University, 1 Brookings Drive, St. Louis, USA
E-mail: ggokel@wustl.edu
Fax: +1 314-362-9298
Tel: +1 314-362-9297

Abstract

Changes in the peptide chain of amphiphilic heptapeptides known to form ion-conducting pores in bilayers dramatically alter transport efficacy and the aggregation number of pore formation.

Graphical abstract: Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles

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Article information

DOI
https://doi.org/10.1039/B514806P
Article type
Communication
Submitted
09 Aug 2005
Accepted
17 Oct 2005
First published
02 Dec 2005

Chem. Commun., 2006, 439-441

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Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles

R. Ferdani, R. Pajewski, J. Pajewska, P. H. Schlesinger and G. W. Gokel, Chem. Commun., 2006, 439 DOI: 10.1039/B514806P

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