© 2014 by John Wiley & Sons, Inc. All rights reserved. This chapter illustrates how an increasing number of studies are taking advantage of the amyloid-like nature of the intracellular aggregates formed in bacteria for a number of different purposes, ranging from the mechanistic analysis of the process of protein aggregation in an in vivo-like environment, to the identification of novel antiamyloidogenic compounds. Protein aggregation is also a major bottleneck during the biotechnological production and purification of proteins, hindering the commercialization of protein-based drugs. Despite it having been observed recurrently that recombinant protein expression in bacterial hosts often leads to aggregation of the target protein into compact aggregated structures known as inclusion bodies (IBs). The IBs formed by different and unrelated proteins shared similar conformational properties, suggesting for the first time that the presence of amyloid-like features could be a common characteristic of bacterial protein deposits.
|Title of host publication||Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells|
|Number of pages||23|
|Publication status||Published - 14 Apr 2014|
- Amyloid aggregation
- Biotechnological production
- Inclusion bodies (IBs)
- Protein-based drugs