A dialysis-based in vitro drug release assay to study dynamics of the drug-protein transfer of temoporfin liposomes
Autor: | Arno Wiehe, Ge F. Gao, Manuela Thurn, Volker Albrecht, Laura Jablonka, Matthias G. Wacker, Christine Janas, Mônica Villa Nova, Chantal M. Wallenwein |
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Přispěvatelé: | Publica |
Jazyk: | angličtina |
Rok vydání: | 2019 |
Předmět: |
Pharmaceutical Science
Biological Availability Context (language use) 02 engineering and technology Plasma protein binding 030226 pharmacology & pharmacy Temoporfin 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Animals Particle Size Active ingredient Liposome Drug Carriers Photosensitizing Agents General Medicine Blood Proteins 021001 nanoscience & nanotechnology Blood proteins Bioavailability Drug Liberation Kinetics Biochemistry chemistry Mesoporphyrins Liposomes Cattle Nanocarriers 0210 nano-technology Biotechnology Protein Binding |
Popis: | Today, a growing number of nanotherapeutics is utilized to deliver poorly soluble compounds using the intravenous route of administration. The drug release and the direct transfer of the active pharmaceutical ingredient to serum proteins plays an important role in bioavailability and accumulation of the drug at the target site. It is closely related to the formation of a protein corona as well as the plasma protein binding of the compound. In the present study, two in vitro drug release methods, the flow-through cell and the dispersion releaser technology, were evaluated with regards to their capability to measure a time-resolved profile of the serum protein binding. In this context, the photosensitizer temoporfin and temoporfin-loaded liposomes were tested. While in the fine capillaries of the flow-through cell a rapid agglomeration of proteins occurred, the dispersion releaser technology in combination with the four-step model enabled the measurement of the transfer of drugs from liposomes to proteins. In presence of 10% of fetal calf serum approximately 20% of the model compound temoporfin were bound to serum proteins within the first 3 h. At higher serum concentration this binding remained stable for approximately 10 h. |
Databáze: | OpenAIRE |
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