Protein immobilization on the surface of liposomes via carbodiimide activation in the presence of N‐hydroxysulfosuccinimide

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Abstract
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 (RCAI 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.