Protein Aggregation in Bacteria

Focuses on the aggregation of recombinant proteins in
bacterial cells in the form of inclusion bodies--and on their
use in biotechnological and medical applications

The first book devoted specifically to the topic of aggregation
in bacteria, Protein Aggregation in Bacteria: Functional and
Structural Properties of Inclusion Bodies in Bacterial Cells
provides a large overview of protein folding and aggregation,
including cell biology and methodological aspects. It summarizes,
for the first time in one book, ideas and technical approaches that
pave the way for a direct use of inclusion bodies in
biotechnological and medical applications.

Protein Aggregation in Bacteria covers:

• Molecular and cellular mechanisms of protein folding,
  aggregation, and disaggregation in bacteria

• Physiological importance and consequences of aggregation for
  the bacterial cell

• Factors inherent to the protein sequence responsible for
  aggregation and evolutionary mechanisms to keep proteins
  soluble

• Structural properties of proteins expressed as soluble
  aggregates and as inclusion bodies within bacterial cells both from
  a methodological point of view and with regard to their similarity
  with amyloids

• Control of the structural and functional properties of
  aggregated proteins and use thereof in biotechnology and
  medicine

Protein Aggregation in Bacteria is ideal for researchers
in protein science, biochemistry, bioengineering, biophysics,
microbiology, medicine, and biotechnology, particularly if they are
related with the production of recombinant proteins and
pharmaceutical science.

Autorentext

SILVIA MARIA DOGLIA, PhD, is Professor of Physics at the
University of Milano-Bicocca, Italy. She received her Laurea degree
in Physics at the University of Milano. She has been Staff Research
Scientist of the Italian National Research Council; Visiting
Scientist at the University of Stockholm; Visiting Professor at the
Universities of Orléans (Fr) and of Reims (Fr). Her research
in Biophysics at the University of Milano-Bicocca is focused on the
study of protein folding and aggregation in vitro and in
situ.

MARINA LOTTI, PhD, is Professor of Biochemistry at the
University of Milano-Bicocca, Italy, where she leads the group
Protein Engineering and Industrial Enzymology, and is the Head of
the Department of Biotechnology and Biosciences. She obtained her
PhD degree at the Max-Planck Institute of Molecular Genetics,
Berlin, and was a researcher of the Italian National Research
Council. Major research topics include the production of
recombinant proteins, protein aggregation, cold-active enzymes, and
intrinsically disordered proteins.

Zusammenfassung

Focuses on the aggregation of recombinant proteins in bacterial cells in the form of inclusion bodiesand on their use in biotechnological and medical applications

The first book devoted specifically to the topic of aggregation in bacteria, Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells provides a large overview of protein folding and aggregation, including cell biology and methodological aspects. It summarizes, for the first time in one book, ideas and technical approaches that pave the way for a direct use of inclusion bodies in biotechnological and medical applications.

Protein Aggregation in Bacteria covers:

• Molecular and cellular mechanisms of protein folding, aggregation, and disaggregation in bacteria
• Physiological importance and consequences of aggregation for the bacterial cell
• Factors inherent to the protein sequence responsible for aggregation and evolutionary mechanisms to keep proteins soluble
• Structural properties of proteins expressed as soluble aggregates and as inclusion bodies within bacterial cells both from a methodological point of view and with regard to their similarity with amyloids
• Control of the structural and functional properties of aggregated proteins and use thereof in biotechnology and medicine
  Protein Aggregation in Bacteria is ideal for researchers in protein science, biochemistry, bioengineering, biophysics, microbiology, medicine, and biotechnology, particularly if they are related with the production of recombinant proteins and pharmaceutical science.

Inhalt

Contributors vii

Preface xi

Introduction to the Wiley Series in Protein and Peptide Science
xiii

1 Fundamentals of Protein Folding 1

Vladimir N. Uversky

2 Recruiting Unfolding Chaperones to Solubilize Misfolded
Recombinant Proteins 63

Rayees U.H. Mattoo and Pierre Goloubinoff

3 Osmolytes as Chemical Chaperones to Use in Protein
Biotechnology 77

Ario de Marco

4 Inclusion Bodies in the Study of Amyloid Aggregation 93

Anna Villar-Piqué and Salvador Ventura

5 Protein Aggregation in Unicellular Eukaryotes 117

Marina Caldara, Joris Winderickx, and Vanessa Franssens

6 Structural Properties of Bacterial Inclusion Bodies 151

Antonino Natalello, Diletta Ami, and Silvia Maria Doglia

7 Residue-Specific Structural Studies of Inclusion Bodies
181

Christian Wasmer, Marielle Wälti, Yongli Chen, and Lei
Wang

8 Biomedical Applications of Bacterial Inclusion Bodies
203

Imma Ratera, Spela Peternel, Joaquin Seras-Franzoso, Olivia
Cano-Garrido, Elena García-Fruitós, Rafael Cubarsí,
Esther Vazquez, José Luis Corchero, Escarlata
Rodríguez-Carmona, Jaume Veciana, and Antonio Villaverde

9 Aggregation of Recombinant Proteins: Understanding Basic
Issues to Overcome Production Bottlenecks 221

Marina Lotti and Loredano Pollegioni

10 Fusion to a Pull-Down Module: Designing Enzymes to Form
Biocatalytically Active Insoluble Aggregates 247

Bernd Nidetzky

Index 263