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首页> 外文期刊>European journal of pharmaceutical sciences >Microcalorimetric studies of the effects on the interactions of human recombinant interferon-alpha2a.
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Microcalorimetric studies of the effects on the interactions of human recombinant interferon-alpha2a.

机译：微量热法研究对人重组干扰素-α2a相互作用的影响。

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The applicability of the physical stability of protein solution monitored by isothermal titration calorimetry (ITC) was evaluated. The second virial coefficient, b2, derived from the dilution enthalpies of protein solution measured by ITC under various experimental conditions was studied. The protein applied in this work is human recombinant interferon-alpha2a (hrIFN-alpha2a), which is a commercial drug applied for the treatment of virus-infected diseases. The results obtained were used to predict the possibility of hrIFN-alpha2a aggregation, and the prediction can be further confirmed by size-exclusion chromatography (SEC). Various factors affecting the stability of protein solution were investigated, for example, temperature, salts, surfactants, and mechanical stress. Specifically, the results show that the dilution enthalpy of hrIFN-alpha2a increased with increasing temperature and NaCl concentration, while b2 decreased, indicating that the attraction between hrIFN-alpha2a molecules was enhanced under these conditions. On studying the effect of mechanical stress, the data obtained reveals that the introduction of centrifugal or vortex force strengthened the attractive forces between hrIFN-alpha2a molecules. These implications were supported by SEC data, demonstrating that the amount of aggregated hrIFN-alpha2a was increased. As a consequence, the methodologies presented in this investigation offer a possibility of monitoring the physical stability of protein solution at various stages of recovery, purification as well as the development of appropriate drug storage formulations.
机译：评估了通过等温滴定量热（ITC）监测的蛋白质溶液物理稳定性的适用性。研究了在各种实验条件下，由ITC测量的蛋白质溶液的稀释焓得出的第二病毒系数b2。这项工作中应用的蛋白质是人重组干扰素-α2a（hrIFN-α2a），这是一种用于治疗病毒感染疾病的商业药物。获得的结果用于预测hrIFN-α2a聚集的可能性，并且该预测可以通过尺寸排阻色谱法（SEC）进一步确认。研究了影响蛋白质溶液稳定性的各种因素，例如温度，盐，表面活性剂和机械应力。具体地，结果表明，随着温度和NaCl浓度的升高，hrIFN-α2a的稀释焓增加，而b2降低，表明在这些条件下hrIFN-α2a分子之间的吸引力增强。通过研究机械应力的影响，获得的数据表明，离心力或涡旋力的引入增强了hrIFN-α2a分子之间的吸引力。 SEC数据支持了这些含义，表明hrIFN-alpha2a的总量增加了。结果，本研究中提出的方法学为监测蛋白质溶液在回收，纯化和开发合适药物储存制剂各个阶段的物理稳定性提供了可能性。

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