Highly monodisperse magnetite nanocrystals (MNC) were synthesized in organic media and transferred to the water phase by ultrasound-assisted ligand exchange with an iminodiacetic phosphonate. The resulting biocompatible magnetic nanoparticles were characterized by transmission electron microscopy, dynamic light scattering, and magnetorelaxometry, indicating that this method allowed us to obtain stable particle dispersions with narrow size distribution and unusually high magnetic resonance T2 contrast power. These nanoparticles were conjugated to a newly designed recombinant monodomain protein A variant, which exhibited a convincingly strong affinity for human and rabbit IgG molecules. Owing to the nature of antibody-protein A binding, tight antibody immobilization occurred through the Fc fragment thus taking full advantage of the targeting potential of bound IgGs. If necessary, monoclonal antibodies could be removed under controlled conditions regenerating the original IgG-conjugatable MNC. As a proof of concept of the utility of our paramagnetic labeling system of human IgGs for biomedical applications, anti-HER-2 monoclonal antibody trastuzumab was immobilized on hybrid MNC (TMNC). TMNC were assessed by immunoprecipitation assay and confocal microscopy effected on HER-2-overexpressing MCF-7 breast cancer cells, demonstrating excellent recognition capability and selectivity for the target membrane receptor. © 2010 American Chemical Society.

Mazzucchelli, S., Colombo, M., De Palma, C., Verderio, P., Coghi, M., Clementi, E., et al. (2010). Single-domain protein A-engineered magnetic nanoparticles: toward a universal strategy to site-specific labeling of antibodies for targeted detection of tumor cells. ACS NANO, 4(10), 5693-5702 [10.1021/nn101307r].

Single-domain protein A-engineered magnetic nanoparticles: toward a universal strategy to site-specific labeling of antibodies for targeted detection of tumor cells

MAZZUCCHELLI, SERENA;COLOMBO, MIRIAM;VERDERIO, PAOLO;COGHI, MARIA DONATA;TORTORA, PAOLO;PROSPERI, DAVIDE
2010

Abstract

Highly monodisperse magnetite nanocrystals (MNC) were synthesized in organic media and transferred to the water phase by ultrasound-assisted ligand exchange with an iminodiacetic phosphonate. The resulting biocompatible magnetic nanoparticles were characterized by transmission electron microscopy, dynamic light scattering, and magnetorelaxometry, indicating that this method allowed us to obtain stable particle dispersions with narrow size distribution and unusually high magnetic resonance T2 contrast power. These nanoparticles were conjugated to a newly designed recombinant monodomain protein A variant, which exhibited a convincingly strong affinity for human and rabbit IgG molecules. Owing to the nature of antibody-protein A binding, tight antibody immobilization occurred through the Fc fragment thus taking full advantage of the targeting potential of bound IgGs. If necessary, monoclonal antibodies could be removed under controlled conditions regenerating the original IgG-conjugatable MNC. As a proof of concept of the utility of our paramagnetic labeling system of human IgGs for biomedical applications, anti-HER-2 monoclonal antibody trastuzumab was immobilized on hybrid MNC (TMNC). TMNC were assessed by immunoprecipitation assay and confocal microscopy effected on HER-2-overexpressing MCF-7 breast cancer cells, demonstrating excellent recognition capability and selectivity for the target membrane receptor. © 2010 American Chemical Society.
No
Articolo in rivista - Articolo scientifico
Scientifica
biolabeling; breast cancer; magnetic nanoparticles; phase transfer; protein A; targeted MRI contrast agents;
Nanobiotecnologie; tumori; biologia molecolare; bioconiugazione; imaging; proteina A; anticorpi;
English
5693
5702
10
Mazzucchelli, S., Colombo, M., De Palma, C., Verderio, P., Coghi, M., Clementi, E., et al. (2010). Single-domain protein A-engineered magnetic nanoparticles: toward a universal strategy to site-specific labeling of antibodies for targeted detection of tumor cells. ACS NANO, 4(10), 5693-5702 [10.1021/nn101307r].
Mazzucchelli, S; Colombo, M; De Palma, C; Verderio, P; Coghi, M; Clementi, E; Tortora, P; Corsi, F; Prosperi, D
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10281/20662
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