Cells have evolved complex and overlapping mechanisms to protect their proteins from aggregation. However, several reasons can cause the failure of such defences, among them mutations, stress conditions and high rates of protein synthesis, all common consequences of heterologous protein production. As a result, in the bacterial cytoplasm several recombinant proteins aggregate as insoluble inclusion bodies. The recent discovery that aggregated proteins can retain native-like conformation and biological activity has opened the way for a dramatic change in the means by which intracellular aggregation is approached and exploited. This paper summarizes recent studies towards the direct use of inclusion bodies in biotechnology and for the detection of bottlenecks in the folding pathways of specific proteins. We also review the major biophysical methods available for revealing fine structural details of aggregated proteins and which information can be obtained through these techniques.

GATTI LANFRANCONI, P., Natalello, A., Ami, D., Doglia, S., Lotti, M. (2011). Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology. THE FEBS JOURNAL, 278(14), 2408-2418 [10.1111/j.1742-4658.2011.08163.x].

Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology

GATTI LANFRANCONI, PIETRO FRANCESCO;NATALELLO, ANTONINO;AMI, DILETTA;DOGLIA, SILVIA MARIA;LOTTI, MARINA
2011

Abstract

Cells have evolved complex and overlapping mechanisms to protect their proteins from aggregation. However, several reasons can cause the failure of such defences, among them mutations, stress conditions and high rates of protein synthesis, all common consequences of heterologous protein production. As a result, in the bacterial cytoplasm several recombinant proteins aggregate as insoluble inclusion bodies. The recent discovery that aggregated proteins can retain native-like conformation and biological activity has opened the way for a dramatic change in the means by which intracellular aggregation is approached and exploited. This paper summarizes recent studies towards the direct use of inclusion bodies in biotechnology and for the detection of bottlenecks in the folding pathways of specific proteins. We also review the major biophysical methods available for revealing fine structural details of aggregated proteins and which information can be obtained through these techniques.
Articolo in rivista - Review Essay
biocatalysis; electron and optical microscopies; fourier transform infrared spectroscopy; inclusion bodies; IB structural properties; native-like conformation; recombinant proteins; stress response
English
2408
2418
11
GATTI LANFRANCONI, P., Natalello, A., Ami, D., Doglia, S., Lotti, M. (2011). Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology. THE FEBS JOURNAL, 278(14), 2408-2418 [10.1111/j.1742-4658.2011.08163.x].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/24373
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