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Why and how protein aggregation has to be studied in vivo

Diletta Ami12, Antonino Natalello1, Marina Lotti1 and Silvia Maria Doglia12*

Author Affiliations

1 Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy

2 Department of Physics “G. Occhialini”, University of Milano-Bicocca, Piazza della Scienza 3, 20126, Milano, Italy

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Microbial Cell Factories 2013, 12:17  doi:10.1186/1475-2859-12-17

Published: 15 February 2013


The understanding of protein aggregation is a central issue in different fields of protein science, from the heterologous protein production in biotechnology to amyloid aggregation in several neurodegenerative and systemic diseases. To this goal, it became more and more evident the crucial relevance of studying protein aggregation in the complex cellular environment, since it allows to take into account the cellular components affecting protein aggregation, such as chaperones, proteases, and molecular crowding. Here, we discuss the use of several biochemical and biophysical approaches that can be employed to monitor protein aggregation within intact cells, focusing in particular on bacteria that are widely employed as microbial cell factories.

Amyloids; Inclusion bodies; Intact cells; Protein aggregation; Spectroscopy