A fast method for assessing the stability of monoclonal antibodies (mAbs) adsorbed on ion exchange resins has been developed. The method exploited a real time polymerase chain reaction equipment to determine the temperature of protein phase transition, i.e., the so called melting temperature, based on differential scanning fluorimetry.

Changes to the melting temperature were screened under various adsorption conditions and correlated with the protein stability upon adsorption.

The method was tested for two different mAbs bound to various types of strong cation exchangers at different pH and loading concentrations. The mAbs destabilized upon adsorption due to strong binding, which manifested itself in aggregate formation and recovery reduction. The phenomenon depended on the resin type and binding conditions. However, regardless of the process conditions and resins used, drop in the melting temperatures to a critical value of about 30° could serve as an indicator of destructive changes in the protein structure in the adsorbed phase. The measurements were simultaneously accomplished for a number of samples with very small material consumption. Therefore, the method may be applied for screening resins and operating variables for a given mAb to exclude conditions that induce structure destabilization and aggregation.

已经开发出一种评估吸附在离子交换树脂上的单克隆抗体（mAb）稳定性的快速方法。该方法利用实时聚合酶链反应设备，基于差示扫描荧光法确定蛋白质相变的温度，即所谓的解链温度。

在各种吸附条件下筛选熔融温度的变化，并将其与吸附时的蛋白质稳定性相关。

测试了该方法中两种不同mAb在不同pH和负载浓度下与各种类型的强阳离子交换剂的结合。由于强结合，mAb在吸附时不稳定，这表现为聚集体形成和回收率降低。该现象取决于树脂类型和结合条件。但是，无论使用何种工艺条件和树脂，熔融温度下降至约30°的临界值都可以用作吸附相中蛋白质结构破坏性变化的指标。同时完成了许多材料消耗非常小的样品的测量。因此，该方法可用于筛选给定mAb的树脂和操作变量，以排除引起结构不稳定和聚集的条件。