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.
Department of Molecular Biology & Pharmacology, Washington University School of Medicine, 660 S. Euclid Avenue, Box 8103, St. Louis, MO 63110, USA.
Riccardo
R
Ferdani
Robert
R
Pajewski
Jolanta
J
Pajewska
Paul H
PH
Schlesinger
George W
GW
Gokel
D001692:Biological Transport; D004295:Dihydroxyphenylalanine / Q000737:chemistry; D005452:Fluoresceins / Q000737:chemistry; D005998:Glycine / Q000737:chemistry*; D007477:Ions; D008051:Lipid Bilayers / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry; D016062:Porosity; D013501:Surface-Active Agents / Q000737:chemistry; D013997:Time Factors
D005452:Fluoresceins; D007477:Ions; D008051:Lipid Bilayers; D008081:Liposomes; D009842:Oligopeptides; D010713:Phosphatidylcholines; D013501:Surface-Active Agents; C024098:6-carboxyfluorescein; D004295:Dihydroxyphenylalanine; C017251:1,2-oleoylphosphatidylcholine; D005998:Glycine