ArticleBinding Mechanism of Doxorubicin in Lon-Exchange Albumin Microcapsules
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2013, International Journal of PharmaceuticsCitation Excerpt :The co-ion is carried along with it in order to maintain electroneutrality, until the chemical potentials are balanced (Jaskari et al., 2001). This phenomenon has also been observed with ion-exchange resins into which the amount of drugs loaded was significantly higher than the amount of ionic binding sites in resins when the highly concentrated drug solutions were loaded (Sawaya et al., 1987). The maximum loading of propranolol in Amberlite™ IRP 69 resin (4.4 mmol/g) was higher than the IEC of resin (3.45 meq/g).
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2012, International Journal of PharmaceuticsCitation Excerpt :This effect cannot be explained by the process of simple diffusion. Albumin is known as an important transport protein and has several binding sites for hydrophobic compounds, which may explain the affinity of albumin for doxorubicin, maintaining the drug within lyophilisomes (Sawaya et al., 1987; Dreis et al., 2007). Albumin-based lyophilisomes may be a suitable delivery system for this drug and doxorubicin loaded lyophilisomes may be prepared upfront and stored at 4 °C or in a lyophilized state.
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2007, European Journal of Pharmaceutical SciencesThe effect of valence on the ion-exchange process: Theoretical and experimental aspects on compound binding/release
2007, Journal of Pharmaceutical SciencesCitation Excerpt :The release of di-COOH was consistently lower than the release of SA across the used fibers and external conditions. The electrostatic interaction between the bound divalent compound and the ion-exchanger is stronger as compared with the monovalent compound (SA) due to the dual site binding.15,21–25 The formed strong interaction hinders the release of di-COOH from the fibers, especially in the case of monovalent extracting electrolyte, by preferring the divalent di-COOH over the chloride-ion (electroselectivity) (Tab. 3,