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Membranotropic properties of the water soluble amino acid and peptide derivatives of fullerene C 60
Author(s) -
Kotelnikova Raisa A.,
Kotelnikov Alexander I.,
Bogdanov Guennady N.,
Romanova Valentina S.,
Kuleshova Elena F.,
Parnes Zinaida N.,
Vol'pin Mark E.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00537-6
Subject(s) - liposome , chemistry , bilayer , lipid bilayer , dipeptide , alanine , peptide , amphiphile , fullerene , phosphatidylcholine , fluorescence , amino acid , metal ions in aqueous solution , biophysics , membrane , organic chemistry , metal , biochemistry , phospholipid , physics , quantum mechanics , copolymer , biology , polymer
The modifying effects of the products of the equimolar addition of dl ‐alanine and dl ‐alanyl‐ dl ‐alanine to fullerene C 60 on the structure and permeability of the lipid bilayer of phosphatidylcholine liposomes has been studied using the luminescence probe technique. It is shown that these water soluble amino acid and dipeptide derivatives of fullerene (C 60 ‐AD) are quenchers of pyrene fluorescence and erythrosine phosphorescence of in both a water solution and liposomes. To study the permeability of the lipid bilayer a procedure based on the triplet probe technique has been developed. It has been found that the C 60 ‐AD derivatives under study are able to localize inside the artificial membrane, to penetrate into the liposomes through the lipid bilayer and to perform activated transmembrane transport of bivalent metal ions.