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Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles

Novel superparamagnetic surface-active maghemite nanoparticles (SAMNs) characterized by a diameter of 10 ± 2 nm were modified with bovine serum amine oxidase, which used rhodamine B isothiocyanate (RITC) adduct as a fluorescent spacer-arm. A fluorescent and magnetically drivable adduct comprised of...

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Autores principales: Sinigaglia, Giulietta, Magro, Massimiliano, Miotto, Giovanni, Cardillo, Sara, Agostinelli, Enzo, Zboril, Radek, Bidollari, Eris, Vianello, Fabio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356201/
https://www.ncbi.nlm.nih.gov/pubmed/22619559
http://dx.doi.org/10.2147/IJN.S28237
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author Sinigaglia, Giulietta
Magro, Massimiliano
Miotto, Giovanni
Cardillo, Sara
Agostinelli, Enzo
Zboril, Radek
Bidollari, Eris
Vianello, Fabio
author_facet Sinigaglia, Giulietta
Magro, Massimiliano
Miotto, Giovanni
Cardillo, Sara
Agostinelli, Enzo
Zboril, Radek
Bidollari, Eris
Vianello, Fabio
author_sort Sinigaglia, Giulietta
collection PubMed
description Novel superparamagnetic surface-active maghemite nanoparticles (SAMNs) characterized by a diameter of 10 ± 2 nm were modified with bovine serum amine oxidase, which used rhodamine B isothiocyanate (RITC) adduct as a fluorescent spacer-arm. A fluorescent and magnetically drivable adduct comprised of bovine serum copper-containing amine oxidase (SAMN–RITC–BSAO) that immobilized on the surface of specifically functionalized magnetic nanoparticles was developed. The multifunctional nanomaterial was characterized using transmission electron microscopy, infrared spectroscopy, mass spectrometry, and activity measurements. The results of this study demonstrated that bare magnetic nanoparticles form stable colloidal suspensions in aqueous solutions. The maximum binding capacity of bovine serum amine oxidase was approximately 6.4 mg g(−1) nanoparticles. The immobilization procedure reduced the catalytic activity of the native enzyme to 30% ± 10% and the Michaelis constant was increased by a factor of 2. We suggest that the SAMN–RITC–BSAO complex, characterized by a specific activity of 0.81 IU g(−1,) could be used in the presence of polyamines to create a fluorescent magnetically drivable H(2)O(2) and aldehydes-producing system. Selective tumor cell destruction is suggested as a potential future application of this system.
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spelling pubmed-33562012012-05-22 Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles Sinigaglia, Giulietta Magro, Massimiliano Miotto, Giovanni Cardillo, Sara Agostinelli, Enzo Zboril, Radek Bidollari, Eris Vianello, Fabio Int J Nanomedicine Original Research Novel superparamagnetic surface-active maghemite nanoparticles (SAMNs) characterized by a diameter of 10 ± 2 nm were modified with bovine serum amine oxidase, which used rhodamine B isothiocyanate (RITC) adduct as a fluorescent spacer-arm. A fluorescent and magnetically drivable adduct comprised of bovine serum copper-containing amine oxidase (SAMN–RITC–BSAO) that immobilized on the surface of specifically functionalized magnetic nanoparticles was developed. The multifunctional nanomaterial was characterized using transmission electron microscopy, infrared spectroscopy, mass spectrometry, and activity measurements. The results of this study demonstrated that bare magnetic nanoparticles form stable colloidal suspensions in aqueous solutions. The maximum binding capacity of bovine serum amine oxidase was approximately 6.4 mg g(−1) nanoparticles. The immobilization procedure reduced the catalytic activity of the native enzyme to 30% ± 10% and the Michaelis constant was increased by a factor of 2. We suggest that the SAMN–RITC–BSAO complex, characterized by a specific activity of 0.81 IU g(−1,) could be used in the presence of polyamines to create a fluorescent magnetically drivable H(2)O(2) and aldehydes-producing system. Selective tumor cell destruction is suggested as a potential future application of this system. Dove Medical Press 2012 2012-05-03 /pmc/articles/PMC3356201/ /pubmed/22619559 http://dx.doi.org/10.2147/IJN.S28237 Text en © 2012 Sinigaglia et al, publisher and licensee Dove Medical Press Ltd. This is an Open Access article which permits unrestricted noncommercial use, provided the original work is properly cited.
spellingShingle Original Research
Sinigaglia, Giulietta
Magro, Massimiliano
Miotto, Giovanni
Cardillo, Sara
Agostinelli, Enzo
Zboril, Radek
Bidollari, Eris
Vianello, Fabio
Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title_full Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title_fullStr Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title_full_unstemmed Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title_short Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
title_sort catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356201/
https://www.ncbi.nlm.nih.gov/pubmed/22619559
http://dx.doi.org/10.2147/IJN.S28237
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