INVESTIGADORES
ALASINO Roxana Valeria
congresos y reuniones científicas
Título:
GANGLIOSIDE MICELLES LOADED WITH ONCOLOGICAL DRUGS CAN BE COATED WITH SPECIFIC ANTIBODIES AS STRATEGY TO IMPROVE TARGETING
Autor/es:
GARRO AG; ALASINO RV; LEONHARD V; HEREDIA V; BELTRAMO DM
Lugar:
Buenos Aires
Reunión:
Jornada; XX Jornadas Anuales de la Sociedad Argentina de Biología (SAB) XVII Jornadas de la Sociedad Uruguaya de Biociencias (SUB) Segundas Jornadas Rioplatenses de Biología; 2018
Institución organizadora:
Sociedad Argentina de Biología
Resumen:
GANGLIOSIDE MICELLES LOADED WITH ONCOLOGICAL DRUGS CANBE COATED WITH SPECIFIC ANTIBODIES AS STRATEGY TO IMPROVE TARGETING Garro AG1, AlasinoRV1,2, Leonhard V1,2, Heredia V1 and Beltramo DM1,2,3. 1 Centro de Excelenciaen Productos y Procesos de Córdoba (CEPROCOR-Córdoba); 2 (CONICET); 3 Cátedrade Biotecnología (FCQs- UCC, Córdoba). E-mail: arielgarro10@gmail.com Efficient and site-specific delivery of therapeutic drugs is a criticalchallenge in clinical treatment of cancer. A common strategy to achieve higherspecificity is modifying surface nanocarriers with specific recognition ligands.Recently, we demonstrated that GM1 micelles carry paclitaxel and doxorubicinwith high efficiency and that and that spontaneously bind to albumin formingGM1-drug-albumin complex. In this work, we show that these micelles, underspecific conditions, can be loaded with antibodies to form the GM1-drug-IgGcomplex that could enhance specific site accumulation. We evaluate theinfluence of temperature and pH to obtain stable GM1-IgG complexes and also ifthe presence of antibodies affects the micellar structure and its capacity toload medications. Under optimal conditions, it is possible to obtain stableGM1-IgG complex until ratios 4/1 (w/w). The DLS and TEM results shows thatGM1-IgG complexes have sizes significantly higher than those of GM1 micelles; whichis directly related to the amount of IgG loaded. This GM1-IgG complex retains theability to encapsulate drugs; however, an adequate sequence must be followedduring the preparation in order to obtain efficient GM1-drug-IgG ternarycomplexes. We also showed that the antibodies of theGM1-IgG complex are located with the Fab region in the external domain of themicelles, maintaining their antigenic recognition properties against solubleand cellular antigens. On the other hand, the IgG of the complex is notdisplaced from the micelles in the presence of albumin.