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Protein immobilization on the surface of liposomes via carbodiimide activation in the presence of N ‐hydroxysulfosuccinimide
Author(s) -
Bogdanov A.A.,
Klibanov A.L.,
Torchilin V.P.
Publication year - 1988
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(88)80854-8
Subject(s) - carbodiimide , liposome , phosphatidylethanolamine , chemistry , covalent bond , phospholipid , biochemistry , phosphatidylcholine , chromatography , organic chemistry , membrane
A method of the covalent immobilization of proteins on the surface of liposomes, containing 10% (by mol) of N ‐glutaryl phosphatidylethanolamine, is described. Carboxylic groups of liposomal N ‐glutaryl phosphatidylethanolamine were activated in the presence of water‐soluble carbodiimide and N ‐hydroxysulfosuccinimide and reacted subsequently with protein amino groups. The liposome‐protein conjugates formed contained up to 5 × 10 −4 mol protein/mol lipid. Lectins (RCA I and WGA) upon immobilization on liposomes retained saccharide specificity and the ability to agglutinate red blood cells. The immobilization of mouse monoclonal IgG in a ratio of 3.5 × 10 −4 mol IgG/mol lipid was achieved. The liposome activation in the absence of N ‐hydroxysulfosuccinimide resulted in a 2‐fold decrease of protein coupling yields.