2. タンパク質凍結乾燥製剤の安定性に及ぼす分子運動性の影響に関する検討(セミナー : 生物資源の保存)

概要

論文の詳細を見る
The molecular mobility of lyophilized formulations containing various polymer excipients was determined by solid state pulsed ^1H-NMR and high resolution ^<13>C-NMR, and discussed in relation to protein stability in the formulations. The critical mobility temperature, T_<mc> of these formulations, at which a Lorentzian relaxation process due to liquid-like polymer protons appeared, varied among the polymer excipients, and increased with decreasing water content and increasing polymer molecular weight. The correlation time, τc, of carbonyl carbon of bovine serum γ-globulin in formulations containing dextran decreased substantially at temperatures above T_<mc> in a similar way as the τc of dextran methin carbon. This suggests that the molecular mobility of protein is enhanced at temperatures above T_<mc> by the increased mobility of dextran molecules. Protein aggregation during the storage of these formulations increased substantially at temperatures above T_<mc>, indicating that storage stability of lyophilized protein formulations is closelv related to their molecular mobility.
低温生物工学会の論文
2000-08-26