ArticleInternational journal of molecular sciences2024
Dendrimer Platforms for Targeted Doxorubicin Delivery-Physicochemical Properties in Context of Biological Responses.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Unravelling the Properties of Fluorescent Ammonium Salts to Obtain Thixotropic Hydrogels with Antitumoral Activity.ACS omega · 2026Article
- Article
- The Optimal Amount of PAMAM G3 Dendrimer in Polyurethane Matrices Makes Them a Promising Tool for Controlled Drug Release.Polymers · 2026Article
- Transfection Technologies for Next-Generation Therapies.Journal of clinical medicine · 2025Review
- A Comprehensive Review of Smart Thermosensitive Nanocarriers for Precision Cancer Therapy.International journal of molecular sciences · 2025Review
- Electrospun Fiber Mats with Metronidazole: Design, Evaluation, and Release Kinetics.The journal of physical chemistry. B · 2025Article
- Theoretical and Experimental Analyses of the Interfacial Mechanism of Dendrimer-Doxorubicin Complexes Formation.Molecular pharmaceutics · 2024Article
- A Novel PAMAM G3 Dendrimer-Based Foam with Polyether Polyol and Castor Oil Components as Drug Delivery System into Cancer and Normal Cells.Materials (Basel, Switzerland) · 2024Article
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Authors and funding
8 authors.
Funding
Abstract
The unique structure of G4.0 PAMAM dendrimers allows a drug to be enclosed in internal spaces or immobilized on the surface. In the conducted research, the conditions for the formation of the active G4.0 PAMAM complex with doxorubicin hydrochloride (DOX) were optimized. The physicochemical properties of the system were monitored using dynamic light scattering (DLS), circular dichroism (CD), and fluorescence spectroscopy. The Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D) method was chosen to determine the preferential conditions for the complex formation. The highest binding efficiency of the drug to the cationic dendrimer was observed under basic conditions when the DOX molecule was deprotonated. The decrease in the zeta potential of the complex confirms that DOX immobilizes through electrostatic interaction with the carrier's surface amine groups. The binding constants were determined from the fluorescence quenching of the DOX molecule in the presence of G4.0 PAMAM. The two-fold way of binding doxorubicin in the structure of dendrimers was visible in the Isothermal calorimetry (ITC) isotherm. Fluorescence spectra and release curves identified the reversible binding of DOX to the nanocarrier. Among the selected cancer cells, the most promising anticancer activity of the G4.0-DOX complex was observed in A375 malignant melanoma cells. Moreover, the preferred intracellular location of the complexes concerning the free drug was found, which is essential from a therapeutic point of view.
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