| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Hinrichs, Wouter
University of Groningen
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (17/17 displayed)
- 2024Combinations of arginine and pullulan reveal the selective effect of stabilization mechanisms on different lyophilized proteinscitations
- 2018The mechanism behind the biphasic pulsatile drug release from physically mixed poly(DL-lactic(-co-glycolic) acid)-based compactscitations
- 2016Compacted Solid Dosage Form
- 2015Protein release from water-swellable poly(d,l-lactide-PEG)-b-poly(ϵ-caprolactone) implantscitations
- 2015Protein Stability during Hot Melt Extrusion
- 2015Size and molecular flexibility of sugars determine the storage stability of freeze-dried proteinscitations
- 2015Protein Stability during Hot Melt Extrusion: The Effect of Extrusion Temperature, Hydrophilicity of Polymers and Sugar Glass Pre-stabilization
- 2015Polymeric formulations for drug release prepared by hot melt extrusioncitations
- 2013Designing CAF-adjuvanted dry powder vaccinescitations
- 2013Unraveling protein stabilization mechanismscitations
- 2012Preparation and physicochemical evaluation of a new tacrolimus tablet formulation for sublingual administrationcitations
- 2010Effect of drug-carrier interaction on the dissolution behavior of solid dispersion tabletscitations
- 2006Characterization of the molecular distribution of drugs in glassy solid dispersions at the nano-meter scale, using differential scanning calorimetry and gravimetric water vapour sorption techniquescitations
- 2005Inulin is a promising cryo- and lyoprotectant for PEGylated lipoplexescitations
- 2004Incorporation of lipophilic drugs in sugar glasses by lyophilization using a mixture of water and tertiary butyl alcohol as solventcitations
- 2003Investigations into the stabilization of drugs by sugar glassescitations
- 2001Inulin glasses for the stabilization of therapeutic proteinscitations
Places of action
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article
Inulin glasses for the stabilization of therapeutic proteins
Abstract
<p>Sugar glasses are widely used to stabilize proteins during drying and subsequent storage. To act successfully as a protectant. the sugars should have a high glass transition temperature (Tg). a poor hygroscopicity, a low crystallization rate, and contain no reducing groups. When freeze drying is envisaged as method of drying, a relatively high Tg of the freeze concentrated fraction (Tg') is preferrable. in this study, whether inulins meet these requirements was investigated. Inulins of various degrees of polymerisation (DP) were evaluated. Trehalose glass was used as a positive control. It was found that the Tg and the Tg' of inulins with a number/weight average DP (DPn/DPw) higher than 5.5/6.0 were higher than those of trehalose glass. Furthermore, inulin glasses showed a similar hygroscopicity to that of trehalose glass but crystallized less rapidly. Less than 6% of the sugar units of inulins with a DPn/DPw higher than 5.5/6.0 contained reducing groups. Trehalose contained no reducing groups. Freeze drying of an alkaline phosphatase solution without protectant induced an almost complete loss of the activity of the protein. In contrast, when inulins with a DPn/DPw higher than 5.5/6.0 or trehalose were used as stabilizer, the activity was fully maintained, also after subsequent storage for 4 weeks at 20 degreesC and 0, 45, or 60% RH, respectively. The stabilizing capacities of inulin with a lower DP and glucose were substantially less pronounced. After storage at 60 degreesC for 6 days, the activity of freeze dried samples containing inulins with a DPn/DPw higher than 5.5/6.0 was still about 50% whereas the activity of samples containing inulin with a lower DP, glucose, or trehalose was completely lost. It is: concluded that inulins with a DPn/DPw higher than 5.5/6.0 meet the physicochemical characteristics to successfully act as protectants for proteins. The stabilizing potential of these inulins was clearly shown using alkaline phosphatase as a model protein. (C) 2001 Elsevier Science B.V. All rights reserved.</p>