Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy

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• 作者：Diletta Ami ; Antonino Natalello ; Geoffrey Taylor ; Giancarlo Tonon and Silvia Maria Doglia
• 关键词：Protein aggregation ; Inclusion bodies ; Heterologous protein production ; FT-IR spectroscopy ; Human growth hormone ; Interferon alpha
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2006
• 出版时间：April 2006
• 年：2006
• 卷：1764
• 期：4
• 页码：793-799
• 全文大小：200 K

文摘

The expression of recombinant human growth hormone (h-GH) and human interferon-alpha-2b (IFN-alpha-2b) in E. coli leads to the formation of insoluble protein aggregates or inclusion bodies (IBs). The secondary structure of these IBs, their corresponding native forms and thermal aggregates were studied by Fourier Transform Infrared (FT-IR) spectroscopy and microspectroscopy. It was demonstrated that residual native-like structures were maintained within IBs at different extents depending on the level of expression, with possible implications in biotechnology. Furthermore, comparison between infrared spectra of thermal aggregates and IBs suggests new insights on the structure of protein aggregates.