INFRARED SPECTROSCOPIC STUDIES OF LYOPHILIZATION-INDUCED AND TEMPERATURE-INDUCED PROTEIN AGGREGATION
INFRARED SPECTROSCOPIC STUDIES OF LYOPHILIZATION-INDUCED AND TEMPERATURE-INDUCED PROTEIN AGGREGATION
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DOI：
10.1002/jps.2600840407
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发表时间：
1995-04-01
影响因子：
3.8
通讯作者：
CARPENTER, JF
中科院分区：
文献类型：
--
作者：
DONG, AC;PRESTRELSKI, SJ;CARPENTER, JF
最近的研究清楚地表明，傅里叶变换红外光谱可以作为一种强有力的工具来研究冷冻干燥过程中蛋白质的稳定性，并优化防止冷冻干燥引起的蛋白质聚集的方法。本综述的目的是对这些主题进行概述，并介绍利用红外光谱研究蛋白质二级结构的方法。我们将首先对处理和解释蛋白质红外光谱的理论和实践进行一般性的总结。然后，我们将回顾目前使用红外光谱来研究蛋白质结构和稳定剂在冷冻干燥过程中的作用的文献。接下来，我们将专门关注蛋白质聚集。蛋白质聚集体中光谱特征的大部分研究和关键分配来自于对高温和低温对蛋白质影响的研究。因此，我们将首先考虑这个话题。最后，我们将总结冻干诱导聚集的最新理论和应用工作。
Recent studies have clearly demonstrated that Fourier transform IR spectroscopy can be a powerful tool for the study of protein stabilization during freeze-drying and for optimizing approaches to prevent lyophilization-induced protein aggregation. The purpose of the current review is to provide an overview of these topics, as well as an introduction to the study of protein secondary structure with IR spectroscopy. We will start with a general summary of the theories and practices for processing and interpreting protein IR spectra. We will then review the current literature on the use of IR spectroscopy to study protein structure and the effects of stabilizers during lyophilization. Next we will concentrate specifically on protein aggregation. The bulk of the research and the key assignments of spectral features in protein aggregates come from studies of the effects of high and low temperature on proteins. Therefore, we will first consider this topic. Finally, we will summarize the recent theoretical and applied work on lyophilization-induced aggregation.