Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles.
Ferdani, Riccardo
Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles. [electronic resource] - Chemical communications (Cambridge, England) Jan 2006 - 439-41 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1359-7345
10.1039/b514806p doi
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
Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles. [electronic resource] - Chemical communications (Cambridge, England) Jan 2006 - 439-41 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1359-7345
10.1039/b514806p doi
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