The β-relaxation associated with the sub-glass transition temperature (T_g,β) is attributed to fast, localised molecular motions which can occur below the primary glass transition temperature (T_g,α). Consistent with T_g,β being observed well-below storage temperatures, the β-relaxation associated motions have been hypothesised to influence protein stability in the solid state and could thus impact the quality of e.g. protein powders for inhalation or reconstitution and injection. Why then do distinct solid state protein formulations with similar aggregation profiles after drying and immediate reconstitution, display different profiles when reconstituted following prolonged storage? Is the value of T_g,β, associated with the β-relaxation process of the system, a reliable parameter for characterising the behaviour of proteins in the solid state? Bearing this in mind, in this work we further explore the different relaxation dynamics of glassy solid state monoclonal antibody formulations using terahertz time-domain spectroscopy and dynamical mechanical analysis. By conducting a 52 week stability study on a series of multi-component spray-dried formulations, an approach for characterising and analysing the solid state dynamics and how these relate to protein stability is outlined.

中文翻译：

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固态蛋白质稳定性的先进预测。

与副玻璃化转变温度（T _g，β）相关的β松弛归因于快速的局部分子运动，该运动可能发生在一次玻璃化转变温度（T _g，α）以下。与在低于储存温度的温度下观察到的T _g，β相一致，已假设β松弛相关运动会影响固态蛋白质的稳定性，从而可能影响例如蛋白质的质量。用于吸入或重组和注射的蛋白粉。为什么干燥和立即重建后具有相似聚集特性的独特固态蛋白质制剂，在长时间存放后进行重构时却显示出不同的特性？是T _g，β的值，与系统的β松弛过程相关，是表征固态蛋白质行为的可靠参数吗？牢记这一点，在这项工作中，我们使用太赫兹时域光谱和动力学力学分析进一步探索了玻璃状固态单克隆抗体制剂的不同弛豫动力学。通过对一系列多组分喷雾干燥制剂进行52周稳定性研究，概述了表征和分析固态动力学以及这些动力学与蛋白质稳定性之间的关系的方法。