Protein immobilization on the surface of liposomes via carbodiimide activation in the presence of N-hydroxysulfosuccinimide.
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 x 10(-4) mol protein/mol lipid. Lectins (RCA1 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 x 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.
Bogdanov
A A
AA
USSR Cardiology Research Center, Academy of Medical Sciences, Moscow.
Klibanov
A L
AL
Torchilin
V P
VP
D001671:Biochemistry / Q000379:methods*; D002234:Carbodiimides; D008081:Liposomes; D011485:Protein Binding; D011506:Proteins; D013388:Succinimides
D002234:Carbodiimides; D008081:Liposomes; D011506:Proteins; D013388:Succinimides; C035761:N-hydroxysulfosuccinimide