The Hidden World of Protein Aggregation

1st Edition, Volume 206 - May 30, 2024
Editors: David B. Teplow, Bahareh Dabirmanesh, Vladimir N. Uversky
Language: English
Hardback ISBN:
9 7 8 - 0 - 4 4 3 - 2 9 3 4 0 - 5
eBook ISBN:
9 7 8 - 0 - 4 4 3 - 2 9 3 4 1 - 2

The Hidden World of Protein Aggregation, Volume 206 provides a comprehensive exploration of protein aggregation, uncovering the factors behind the formation of amorphous aggreg… Read more

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The Hidden World of Protein Aggregation, Volume 206 provides a comprehensive exploration of protein aggregation, uncovering the factors behind the formation of amorphous aggregates and ordered structures called amyloid fibrils. It delves into the advantages and disadvantages of protein aggregates, addressing topics such as cytotoxicity and disorders linked to misfolding. Specific chapters in this release include Protein Aggregation: An Overview, Pathways of Amyloid Fibril Formation and Aggregation, Factors Influencing Amyloid Fibril Formation, Morphological Features and Types of Aggregated Structures, Each big journey starts with a first step: Importance of Oligomerization, Liquid-Liquid Phase Separation as Triggering Factor of Fibril Formation, and more.

Additional sections cover Experimental Techniques for Detecting and Evaluating the Amyloid Fibrils, Prediction of Protein Aggregation, Amyloid Fibril Cytotoxicity and Associated Disorders, Inhibitors of Amyloid Fibril Formation, Therapeutic Approaches in Proteinopathies, Functional Amyloids, Biotechnological Applications of Amyloid Fibrils, and The Hidden World of Protein Aggregation.

Cover image
Title page
Table of Contents
Copyright
Contributors
Preface
Abstract
Chapter One: Protein aggregation: An overview
Abstract
1 Brief introduction to protein aggregation phenomenon
2 A brief historical overview
3 Concluding remark
References
Chapter Two: Pathways of amyloid fibril formation and protein aggregation
Abstract
1 Introduction
2 Physicochemical features of proteins
3 Protein folding theories
4 Folding kinetics and mechanisms
5 Protein folding models
6 The folding funnels and energy landscape
7 Protein folding pathways
8 Structure formation and collapse
9 Multiple pathways for the chain collapse reaction
10 Protein misfolding and aggregation
11 Factors affecting aggregation
12 Order/disorder determinants to prevent aggregation
13 Mechanism of amyloid fibril production
14 The energy landscape of amyloid fibrils and aggregation
15 Concluding remarks
References
Chapter Three: Factors influencing amyloid fibril formation
Abstract
1 Introduction
2 Effect of intrinsic factors on protein aggregation
3 Effect of extrinsic factors on protein aggregation
4 Concluding remarks
References
Chapter Four: Morphological features and types of aggregated structures
Abstract
1 Introduction
2 Types of protein aggregates
3 Structure of amyloid fibrils
4 Amino acid ladders for packing and stability of amyloid fibrils
5 Structural polymorphism of amyloid fibrils
6 Concluding remarks
References
Chapter Five: Each big journey starts with a first step: Importance of oligomerization
Abstract
1 Introduction
2 Mechanism of fibril and oligomer formation
3 Intrinsic and extrinsic triggering factors for oligomerization
4 Oligomeric intermediates in fibril formation pathway
5 Structural and morphological features of amyloid oligomers
6 Mechanism of toxicity of oligomers
7 Functional oligomers
8 Antimicrobial peptides oligomerization
9 Concluding remarks
References
Chapter Six: Liquid-liquid phase separation as triggering factor of fibril formation
Abstract
1 Basic principle of LLPS
2 LLPS in microorganisms
3 Biological functions of LLPS
4 Pathological functions of LLPS
5 Control and regulation of LLPS
6 Methods to study
7 LLPS databases
References
Chapter Seven: Experimental techniques for detecting and evaluating the amyloid fibrils
Abstract
1 Introduction
2 Hydrodynamic methods
3 Calorimetry-based methods
4 Chromatographic methods
5 Electrophoretic methods
6 Spectroscopic methods
7 Scattering methods
8 Imaging-based methods
9 Radio imaging
10 Magnetic resonance imaging (MRI)
11 Conclusions
References
Chapter Eight: Prediction of protein aggregation
Abstract
1 Introduction
2 Databases for protein aggregation
3 In silico approaches and methods to study protein aggregation
4 Prediction of the tendency of globular protein structures to aggregate
5 Concluding remarks
References
Chapter Nine: Amyloid fibril cytotoxicity and associated disorders
Abstract
1 Introduction
2 Systemic amyloid diseases
3 Localized amyloid diseases
4 Concluding remarks
References
Chapter Ten: Inhibitors of amyloid fibril formation
Abstract
1 Introduction
2 Small molecule inhibitors
3 Polymeric inhibitors
4 Non-detergent sulfobetaine
5 Nanomaterials
6 Metal-chelating inhibitors
7 High hydrostatic pressure and low temperature
8 Laser irradiation
9 Ultrasonic waves
10 Using biomolecule as a strategy for inhibition of amyloid formation
11 Concluding remarks
References
Chapter Eleven: Therapeutic approaches in proteinopathies
Abstract
1 Introduction
2 Therapeutic for amyloid diseases
3 Regulatory considerations for amyloid disease therapies
4 Concluding remarks
References
Chapter Twelve: Functional amyloids
Abstract
1 Introduction
2 Functional amyloids in microorganisms
3 Function of amyloids in mammalians
4 Functional amyloids in plants
5 Concluding remarks
References
Chapter Thirteen: Biotechnological applications of amyloid fibrils
Abstract
1 Introduction
2 Biotechnology applications of amyloid fibrils
3 Concluding remarks
References
Chapter Fourteen: The hidden world of protein aggregation
Abstract
1 A journey of protein aggregation
2 Remaining mysteries of protein aggregation
3 Emerging therapeutic strategies
4 Application of functional amyloids
5 Forthcoming techniques for the protein aggregation research
References
Index

David B. Teplow

David B. Teplow, Ph.D., is a Professor of Neurology, Emeritus, at UCLA and an internationally recognized leader in efforts to understand and treat Alzheimer's disease. Dr. Teplow's group has used a multi-disciplinary approach to determine how neurotoxic peptides, such as the amyloid β-protein (Alzheimer's disease) and α-synuclein (Parkinson’s disease), form neurotoxic structures that kill neurons and to develop the means to block these processes. Dr. Teplow received undergraduate training at UC Berkeley; a Ph.D. from the University of Washington; and was a postdoctoral scholar at Caltech. Before coming to UCLA, Dr. Teplow was a faculty member in the Department of Neurology, Harvard Medical School. Dr. Teplow has published >250 peer-reviewed articles, books and book chapters, and commentaries, in addition to serving on numerous national and international scientific advisory boards. Dr. Teplow was a founding editor of the Journal of Molecular Neuroscience and Current Chemical Biology, He is Co-Editor-in-Chief of the Elsevier serial Progress in Molecular Biology and Translational Science and is Associate Editor-in-Chief of the American Journal of Neurodegenerative Disease.

Affiliations and expertise

Department of Neurology, David Geffen School of Medicine, UCLA, Los Angeles, CA, USA

Bahareh Dabirmanesh

Bahareh Dabirmanesh received her Ph.D. in Biochemistry from Tarbiat Modares University (Tehran-Iran) in 2013. Following the completion of her doctoral studies, she joined the University as an academic member pursuing both academic and research activities within the Department of Biochemistry, Faculty of Biological Sciences. During this period, she undertook the responsibilities of a supervisor or advisor for a considerable number of master's and PhD theses. Since 2022, she has held the position of associate professor. Her research interests are mainly focused on protein engineering, macromolecular interactions, structure-function relation, amyloidogenic proteins, Biotherapeutics, protein pathways and signaling cascades

Affiliations and expertise

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran-Iran

Vladimir N. Uversky

Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, FAIMBE, Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, moved to the University of California Santa Cruz. In 2004, joined the Indiana University−Purdue University Indianapolis as a Senior Research Professor. Since 2010, Professor Uversky is with USF, where he works on various aspects of protein intrinsic disorder phenomenon and on analysis of protein folding and misfolding processes. Prof. Uversky has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He is also serving as an editor in a number of scientific journals. He was a co-founder of the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference. Prof. Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.

Affiliations and expertise

PhD, DSc, FRSB, FRSC, FAIMBE, Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida

Life Sciences

Physical Sciences & Engineering

Social Sciences & Humanities

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The Hidden World of Protein Aggregation

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David B. Teplow

Bahareh Dabirmanesh

Vladimir N. Uversky

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