The Experts below are selected from a list of 186 Experts worldwide ranked by ideXlab platform
John F Carpenter - One of the best experts on this subject based on the ideXlab platform.
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effects of solution conditions processing parameters and Container Materials on aggregation of a monoclonal antibody during freeze thawing
Journal of Pharmaceutical Sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:ABSTRACT Freeze–thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze–thawing is protein aggregation. We studied the effects of freeze–thawing on aggregation of an IgG 2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze–thawing increased with decreasing pH, which correlated well with T m values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
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Effects of solution conditions, processing parameters, and Container Materials on aggregation of a monoclonal antibody during freeze–thawing
Journal of pharmaceutical sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:Freeze-thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze-thawing is protein aggregation. We studied the effects of freeze-thawing on aggregation of an IgG2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze-thawing increased with decreasing pH, which correlated well with Tm values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
Lisa A Kueltzo - One of the best experts on this subject based on the ideXlab platform.
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effects of solution conditions processing parameters and Container Materials on aggregation of a monoclonal antibody during freeze thawing
Journal of Pharmaceutical Sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:ABSTRACT Freeze–thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze–thawing is protein aggregation. We studied the effects of freeze–thawing on aggregation of an IgG 2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze–thawing increased with decreasing pH, which correlated well with T m values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
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Effects of solution conditions, processing parameters, and Container Materials on aggregation of a monoclonal antibody during freeze–thawing
Journal of pharmaceutical sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:Freeze-thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze-thawing is protein aggregation. We studied the effects of freeze-thawing on aggregation of an IgG2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze-thawing increased with decreasing pH, which correlated well with Tm values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
Thamir K Ibrahim - One of the best experts on this subject based on the ideXlab platform.
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Corrosion effect of phase change Materials in solar thermal energy storage application
Renewable and Sustainable Energy Reviews, 2017Co-Authors: Anusuiah Vasu, Abdul A. Abdullah, Ftwi Yohaness Hagos, W H Azmi, Rizalman Mamat, M. M. Noor, Thamir K IbrahimAbstract:The thermal energy storage (TES) system using phase change Materials (PCMs) has been studied since past three decades. PCMs are widely used in heat storage applications due to their high storage density, as well as the wide range of melting and solidifying temperatures. Nevertheless, the main disadvantage of PCMs, especially salt hydrates, is their corrosive behavior with Container Materials. PCMs are normally encapsulated in Containers, hence the compatibility of the Container Materials with PCM plays an important role. As such, this paper summarizes the investigations made on the corrosion behavior of PCM in various applications, besides suggesting ways to reduce (or rectify) the effect for long term successful energy storage. Moreover, PCM-storage Material interaction in the latent heat TES system is important as the issue of corrosion affects the life of the Container, as well as the performance of TES. The compatibility of the most commonly used PCMs with several major Container Materials was reviewed and it was revealed that stainless steel has emerged as the most compatible storage Container Material among others. On the other hand, aluminum was found to be corrosive when it is used with salt hydrates. Nonetheless, some contradictory articles are reported that several salt hydrates demonstrated compatibility with Container Materials. Corrosion causes thinning of cross sectional area of Materials, making it brittle thus leading to an easy collapse. This situation is even more critical mainly in large scale concentrating solar thermal power plants. Hence, with the fact that there are currently large scale power plants employing TES under operation and under construction; issues pertaining to PCM-storage Material compatibility should be properly and accurately addressed. Therefore, more research work is recommended in the area of finding new eutectics and less corrosive Container Material(s).
Wei Wang - One of the best experts on this subject based on the ideXlab platform.
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effects of solution conditions processing parameters and Container Materials on aggregation of a monoclonal antibody during freeze thawing
Journal of Pharmaceutical Sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:ABSTRACT Freeze–thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze–thawing is protein aggregation. We studied the effects of freeze–thawing on aggregation of an IgG 2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze–thawing increased with decreasing pH, which correlated well with T m values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
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Effects of solution conditions, processing parameters, and Container Materials on aggregation of a monoclonal antibody during freeze–thawing
Journal of pharmaceutical sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:Freeze-thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze-thawing is protein aggregation. We studied the effects of freeze-thawing on aggregation of an IgG2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze-thawing increased with decreasing pH, which correlated well with Tm values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
Theodore W Randolph - One of the best experts on this subject based on the ideXlab platform.
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effects of solution conditions processing parameters and Container Materials on aggregation of a monoclonal antibody during freeze thawing
Journal of Pharmaceutical Sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:ABSTRACT Freeze–thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze–thawing is protein aggregation. We studied the effects of freeze–thawing on aggregation of an IgG 2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze–thawing increased with decreasing pH, which correlated well with T m values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.
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Effects of solution conditions, processing parameters, and Container Materials on aggregation of a monoclonal antibody during freeze–thawing
Journal of pharmaceutical sciences, 2008Co-Authors: Lisa A Kueltzo, Theodore W Randolph, Wei Wang, John F CarpenterAbstract:Freeze-thawing is a potentially damaging stress to which therapeutic proteins can be exposed deliberately during storage of bulk drug substance, and accidentally because of mishandling of commercial product during shipping and/or storage. The primary route of degradation induced by freeze-thawing is protein aggregation. We studied the effects of freeze-thawing on aggregation of an IgG2 monoclonal antibody, examining solution conditions (pH, and the presence or absence of 150 mM KCl), protein concentration, cooling and warming rates, and Container type and Material. In addition, we determined the effect of pH and KCl on protein tertiary structure and thermal stability with second derivative UV spectroscopy. In general, aggregation of the antibody during freeze-thawing increased with decreasing pH, which correlated well with Tm values. Aggregation was most prevalent at pH 3 and 4, with potential mechanisms involving both the formation of aggregation-prone conformational states as well as adsorption to and denaturation at various interfaces. Although all the parameters examined demonstrated some effect on the formation of soluble aggregates, the effect of Container Material was especially pronounced. Samples stressed in plastic or glass Containers contained low amounts of aggregate. Storage in Teflon or commercial freezing Containers, however, led to significantly higher levels of aggregate formation.