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Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity
- Source :
-
International Journal of Pharmaceutics . May2007, Vol. 336 Issue 2, p276-283. 8p. - Publication Year :
- 2007
-
Abstract
- Abstract: A novel method for synthesis of anti-EGFR immunoliposomes using folate–folate binding protein (FBP) affinity is described. An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were prepared by polycarbonate membrane extrusion. Anti-EGFR immunoliposomes were then obtained by combining FBP-C225 and folate-liposomes and evaluated for uptake and cytotoxicity in EGFR-overexpressing U87 human glioblastoma cells. Anti-EGFR immunoliposomes constructed via folate–FBP affinity exhibited excellent stability under physiological pH, and quickly released the bound FBP-C225 upon low pH (pH 3.5) treatment. Flow cytometry and fluorescence microscopy showed similar receptor-specific binding and internalization for both folate–FBP affinity-coupled and covalently coupled C225-immunoliposomes, but not for the non-targeted IgG-immunoliposomes. C225-immunoliposomes loaded with anticancer drug doxorubicin were more cytotoxic than non-targeted immunoliposomes in EGFR-overexpressing U87 glioma cells. Folate–FBP affinity is a potential method for construction of immunoliposomes and may have applications in synthesis of targeted drug carriers in general. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 03785173
- Volume :
- 336
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- International Journal of Pharmaceutics
- Publication Type :
- Academic Journal
- Accession number :
- 24970296
- Full Text :
- https://doi.org/10.1016/j.ijpharm.2006.12.007