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Original Research

Human serum albumin nanoparticles as an efficient noscapine drug delivery system for potential use in breast cancer: preparation and in vitro analysis

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Pages 525-532 | Published online: 15 Sep 2010

Figures & data

Figure 1 Scanning electron micrograph of glutaraldehyde crosslinked nanoparticles prepared at pH 8, 60k resolution. The nanoparticles were found to be of uniform size and narrow size distribution.

Figure 1 Scanning electron micrograph of glutaraldehyde crosslinked nanoparticles prepared at pH 8, 60k resolution. The nanoparticles were found to be of uniform size and narrow size distribution.

Figure 2 Effect of glutaraldehyde concentration on diameter and polydispersity index of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 2 Effect of glutaraldehyde concentration on diameter and polydispersity index of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 3 Effect of pH on diameter and polydispersity index of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein.

Figure 3 Effect of pH on diameter and polydispersity index of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein.

Figure 4 Stability of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles over 5 days. Particle size was monitored. Noscapine-loaded HSA nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 4 Stability of noscapine (5 mg/mL) loaded human serum albumin (HSA) nanoparticles over 5 days. Particle size was monitored. Noscapine-loaded HSA nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 5 Noscapine encapsulation of human serum albumin nanoparticles (50 mg/mL) in dependence on noscapine concentration.

Figure 5 Noscapine encapsulation of human serum albumin nanoparticles (50 mg/mL) in dependence on noscapine concentration.

Figure 6 Drug release profile of noscapine-loaded human serum albumin (HSA) nanoparticles (noscapine concentration 5–15 mg/mL) over predetermined time intervals. Noscapine-loaded HSA nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 6 Drug release profile of noscapine-loaded human serum albumin (HSA) nanoparticles (noscapine concentration 5–15 mg/mL) over predetermined time intervals. Noscapine-loaded HSA nanoparticles prepared with 10 mM NaCl solution and 100 mg of HSA protein at pH 8.

Figure 7 Breast cancer efficiency of human serum albumin (HSA) nanoparticles-loaded with noscapine (5–15 mg/mL concentration) and controls (drug-free nanoparticles). Nanoparticle concentrations of 50 μg/mL were seeded in SK-BR-3 breast cancer cell line incubated at 24, 48, 72, 96, and 144 h.

Figure 7 Breast cancer efficiency of human serum albumin (HSA) nanoparticles-loaded with noscapine (5–15 mg/mL concentration) and controls (drug-free nanoparticles). Nanoparticle concentrations of 50 μg/mL were seeded in SK-BR-3 breast cancer cell line incubated at 24, 48, 72, 96, and 144 h.