Why and how protein aggregation has to be studied in vivo

Microbial Cell Factories

Commentary

Marina Lotti¹  Antonino Natalello¹  Silvia Maria Doglia²  Diletta Ami² 

[1] Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy;Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy;Department of Physics “G. Occhialini”, University of Milano-Bicocca, Piazza della Scienza 3, 20126, Milano, Italy;

关键词: Amyloids;    Inclusion bodies;    Intact cells;    Protein aggregation;    Spectroscopy;   

DOI  :  10.1186/1475-2859-12-17

 received in 2013-02-04, accepted in 2013-02-07,  发布年份 2013

来源: Springer

【 摘 要 】

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.

【 授权许可】

Unknown   
© Ami et al.; licensee BioMed Central Ltd. 2013. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.