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

FEBS Letters

Torchilin, V.P.¹  Bogdanov, A.A.¹  Klibanov, A.L.¹ 

[1]Institute of Experimental Cardiology, USSR Cardiology Research Center, Academy of Medical Sciences, 3-d Cherepkovsky 15 A, 121552 Moscow, USSR

关键词: Liposome;    N-Hydroxysulfosuccinimide;    Carbodiimide;    Lectin;    Monoclonal antibody;    Immobilization;    WGA;    wheat germ agglutinin;    RCAI;    agglutinin from Ricinus communis;    Con A;    concanavalin A;    HoSu(SO− 3)Na+ N-hydroxysulfosuccinimide;    sodium salt;    EDC;    1-ethyl-3-(3-dimethylaminopropyl) carbodiimide;    DPPC;    L-α-phosphatidylcholine dipalmitoyl;    PE;    phosphatidylethanolamine;    DPPE;    L-α-phosphatidylethanolamine dipalmitoyl;    SPDP;    N-hydroxysuccinimidyl 3-(2-pyridyldithio)propionate;    BBS;    50 mM sodium tetraborate;    0.1 M NaCl;    pH 7.5;    MesBS;    5 mM 2-(N-morpholinoethane) sulfonic acid;    0.15 M NaCl;    pH 5.5;    SUV;    small unilamellar vesicle;    REV;    reverse-phase evaporation vesicle;   

DOI  :  10.1016/0014-5793(88)80854-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown