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

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.

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2006-01 (4), p.439-441
Main Authors: Ferdani, Riccardo, Pajewski, Robert, Pajewska, Jolanta, Schlesinger, Paul H, Gokel, George W
Format: Article
Language:English
Subjects:
Biological Transport
Dihydroxyphenylalanine - chemistry
Fluoresceins - chemistry
Glycine - chemistry
Ions
Lipid Bilayers - chemistry
Liposomes - chemistry
Oligopeptides - chemistry
Phosphatidylcholines - chemistry
Porosity
Surface-Active Agents - chemistry
Time Factors
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Description
Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/b514806p