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Research Article

Preparation of magnetically responsive albumin nanospheres and in vitro drug release studies

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Pages 18-26 | Received 20 Oct 2012, Accepted 17 Jan 2013, Published online: 18 Feb 2013

Figures & data

Table I. DIC and DIE calculations, mean particle size and PDI of nanoparticles.

Figure 1. Particle size and (A) desolvation efficiency of BSA-NPs at different BSA concentrations; (B) DOX incorporation efficiency of DOX-BSA-NPs at different DOX concentrations; and (C) DOX incorporation efficiency of M-DOX-BSA-NPs at different magnetite concentrations.

Figure 1. Particle size and (A) desolvation efficiency of BSA-NPs at different BSA concentrations; (B) DOX incorporation efficiency of DOX-BSA-NPs at different DOX concentrations; and (C) DOX incorporation efficiency of M-DOX-BSA-NPs at different magnetite concentrations.

Figure 2. SEM images of (A) empty, (B) DOX-loaded and (C) DOX-unloaded magnetic albumin nanoparticles.

Figure 2. SEM images of (A) empty, (B) DOX-loaded and (C) DOX-unloaded magnetic albumin nanoparticles.

Figure 3. AFM images of DOX-loaded magnetic albumin nanoparticles: (A) 2D and (B) 3D pictures.

Figure 3. AFM images of DOX-loaded magnetic albumin nanoparticles: (A) 2D and (B) 3D pictures.

Figure 4. XRD spectrum of the (A) BSA-NPs and (B) M-BSA-NPs.

Figure 4. XRD spectrum of the (A) BSA-NPs and (B) M-BSA-NPs.

Figure 5. Magnetization curve of M-DOX-BSA nanoparticles.

Figure 5. Magnetization curve of M-DOX-BSA nanoparticles.

Figure 6. In vitro release profile of DOX from (A) M-DOX-BSA nanoparticles cross-linked different GA ratio and (B) M-DOX-BSA nanoparticles in PBS medium with the absence or presence of proteolytic enzyme at pH 5, 6 and 7.4.

Figure 6. In vitro release profile of DOX from (A) M-DOX-BSA nanoparticles cross-linked different GA ratio and (B) M-DOX-BSA nanoparticles in PBS medium with the absence or presence of proteolytic enzyme at pH 5, 6 and 7.4.

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