Related Experiment Video
Updated: Feb 2, 2026

Microfluidic Device for the Separation of Non-Metastatic MCF-7 and Non-Tumor MCF-10A Breast Cancer Cells Using AC Dielectrophoresis
Published on: August 11, 2022
Surface-tailored anti-HER2/neu-solid lipid nanoparticles for site-specific targeting MCF-7 and BT-474 breast cancer
Eliana B Souto1, Slavomira Doktorovova2, Joana R Campos2
1Department of Pharmaceutical Technology, Faculty of Pharmacy, University of Coimbra (FFUC), Pólo das Ciências da Saúde, Azinhaga de Santa Comba, 3000-548 Coimbra, Portugal; CEB - Centre of Biological Engineering, University of Minho, Campus de Gualtar 4710-057 Braga, Portugal.
Abstract:
CAB51, a compact antibody against human epithelial growth receptor 2 (HER2, ErbB2), has been linked to cationic Solid Lipid Nanoparticles (SLN) via streptavidin-biotin interaction and their targeting potential evaluated against breast cancer cells. The amount of streptavidin and biotinylated antibody was optimised by monitoring the mean complex size (intensity weighed average diameter), polydispersity index and immediate stability in phosphate buffer saline (PBS). The effect on MCF-7 and BT-474 cells was evaluated at concentrations of 0.01 mg/mL and 0.1 mg/mL (counted as solid lipid). Streptavidin adsorption onto SLN surface had no influence on cell viability. Linking the antibody showed a synergistic effect on cell viability at lowest concentration tested (0.01 mg/mL) which was lower than that observed after exposure to SLN alone or antibody alone. At the higher tested concentration (0.1 mg/mL), the observed toxicity was entirely governed by the inherent toxicity of the SLN themselves. Streptavidin adsorption had no effect on accumulation in cells, while the antibody-containing complexes showed clearly increased internalisation in both cell lines. In HER2/neu positive BT-474 higher internalisation was observed than in HER2/neu negative MCF-7.
Insights
Antibody-linked solid lipid nanoparticles (SLN) targeting HER2 receptors enhanced cancer cell uptake. This novel approach shows promise for targeted breast cancer therapy, with increased internalization in HER2-positive cells.
Area of Science:
- Nanotechnology
- Biomedical Engineering
- Oncology
Background:
- Solid Lipid Nanoparticles (SLN) are investigated for drug delivery.
- Targeting cancer cells with specific antibodies can improve therapeutic efficacy.
- Human Epidermal Growth Factor Receptor 2 (HER2) is a key target in breast cancer.
Purpose of the Study:
- To develop and evaluate antibody-conjugated SLN for targeted delivery to HER2-expressing breast cancer cells.
- To optimize the conjugation of a compact antibody (CAB51) to SLN via streptavidin-biotin interaction.
- To assess the cellular uptake and cytotoxic effects of these targeted nanoparticles.
Main Methods:
- Conjugation of CAB51 antibody to cationic SLN using streptavidin-biotin technology.
- Optimization of streptavidin and biotinylated antibody loading by analyzing particle size, polydispersity, and stability.
- Evaluation of cellular uptake and viability in HER2-positive (BT-474) and HER2-negative (MCF-7) breast cancer cell lines.
Main Results:
- Streptavidin adsorption alone did not affect cell viability.
- Antibody-conjugated SLN demonstrated a synergistic effect on cell viability at low concentrations.
- Higher cellular internalization of antibody-containing SLN was observed in both cell lines, particularly in HER2-positive BT-474 cells.
Conclusions:
- Antibody-conjugated SLN effectively target and are internalized by breast cancer cells, especially those overexpressing HER2.
- This targeted delivery system shows potential for enhanced breast cancer therapy.
- The optimization of nanoparticle conjugation is crucial for effective targeted drug delivery.
Related Concept Videos
Structures of Solids
Cell-surface Signaling
Targeted Cancer Therapies
There are several types of targeted therapies against...
Metallic Solids
All metallic solids exhibit high thermal and electrical conductivity, metallic luster, and malleability....
What are Lipids?
Lipid Digestion

