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

Riccardo Ferdani, Robert Pajewski, Jolanta Pajewska, Paul H. Schlesinger, George W. Gokel

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish
Pages (from-to)439-441
Number of pages3
JournalChemical Communications
Issue number4
DOIs
StatePublished - 2006

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