Core-shell gold nanoparticles [AuNPs], stabilized with a hydrophilic polymer, poly(3-dimethylammonium-1-propyne hydrochloride) [PDMPAHCl], have been used for the immobilization of bovine serum amine oxidase [BSAO]. The functionalized surface of the hybrid nanoparticles is pH responsive, due to the presence of aminic groups that carry out a double role: on one hand they act as ligands for the gold nanoparticle surface, allowing the colloidal stabilization and, on the other hand, they give a hydrophilic characteristic to the whole colloidal suspension. The core-shell nanoparticles [Au@PDMPAHCl] have been characterized by using UV-vis and X-ray photoelectron spectroscopy, DLS, ζ-potential measurements and by FE-TEM microscopy. BSAO enzyme can be loaded by non-covalent immobilization onto Au@PDMPAHCl nanoparticles up to 70% in weight, depending on the pH values of the environmental medium. Activity tests on Au@PDMPAHCl-BSAO bioconjugates confirm an enzymatic activity up to 40%, with respect to the free enzyme activity. Moreover, our results show that loading and enzymatic activity are rather interrelated characteristics and that, under appropriate polymer concentration and pH conditions, a satisfactory compromise can be reached. These results, as a whole, indicate that Au@PDMPAHCl-BSAO bioconjugate systems are promising for future biomedical applications.

Bioconjugation of gold-polymer core-shell nanoparticles with bovine serum amine oxidase for biomedical applications / Venditti, I; Hassanein, T. F.; Fratoddi, I.; Fontana, L.; Battocchio, C.; Rinaldi, F.; Carafa, M.; Marianecci, C.; Diociaiuti, M.; Agostinelli, E.; Cametti, C.; Russo, M. V.. - In: COLLOIDS AND SURFACES. B, BIOINTERFACES. - ISSN 0927-7765. - STAMPA. - 134:(2015), pp. 314-321. [10.1016/j.colsurfb.2015.06.052]

Bioconjugation of gold-polymer core-shell nanoparticles with bovine serum amine oxidase for biomedical applications

Venditti, I;Fratoddi, I.
;
Rinaldi, F.;Carafa, M.;Marianecci, C.;Agostinelli, E.;Cametti, C.;
2015

Abstract

Core-shell gold nanoparticles [AuNPs], stabilized with a hydrophilic polymer, poly(3-dimethylammonium-1-propyne hydrochloride) [PDMPAHCl], have been used for the immobilization of bovine serum amine oxidase [BSAO]. The functionalized surface of the hybrid nanoparticles is pH responsive, due to the presence of aminic groups that carry out a double role: on one hand they act as ligands for the gold nanoparticle surface, allowing the colloidal stabilization and, on the other hand, they give a hydrophilic characteristic to the whole colloidal suspension. The core-shell nanoparticles [Au@PDMPAHCl] have been characterized by using UV-vis and X-ray photoelectron spectroscopy, DLS, ζ-potential measurements and by FE-TEM microscopy. BSAO enzyme can be loaded by non-covalent immobilization onto Au@PDMPAHCl nanoparticles up to 70% in weight, depending on the pH values of the environmental medium. Activity tests on Au@PDMPAHCl-BSAO bioconjugates confirm an enzymatic activity up to 40%, with respect to the free enzyme activity. Moreover, our results show that loading and enzymatic activity are rather interrelated characteristics and that, under appropriate polymer concentration and pH conditions, a satisfactory compromise can be reached. These results, as a whole, indicate that Au@PDMPAHCl-BSAO bioconjugate systems are promising for future biomedical applications.
2015
BSAO; core-shell nanoparticles; gold nanoparticles; biotechnology; colloid and surface chemistry; physical and theoretical chemistry; surfaces and interfaces
01 Pubblicazione su rivista::01a Articolo in rivista
Bioconjugation of gold-polymer core-shell nanoparticles with bovine serum amine oxidase for biomedical applications / Venditti, I; Hassanein, T. F.; Fratoddi, I.; Fontana, L.; Battocchio, C.; Rinaldi, F.; Carafa, M.; Marianecci, C.; Diociaiuti, M.; Agostinelli, E.; Cametti, C.; Russo, M. V.. - In: COLLOIDS AND SURFACES. B, BIOINTERFACES. - ISSN 0927-7765. - STAMPA. - 134:(2015), pp. 314-321. [10.1016/j.colsurfb.2015.06.052]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/805265
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