The Hidden World of Protein Aggregation
- 1st Edition, Volume 206 - May 30, 2024
- Imprint: Academic Press
- 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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Request a sales quoteThe 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.
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.
- Provides an introduction to the folding of protein and associated conditions leading to aggregation and linked pathology
- Discusses structural biology and computational methodologies for analysis of protein (mis)folding and aggregation
- Describes functional amyloids and their biotechnological applications
Researchers interested in problems related to amyloid formation and protein folding/mis-folding. Scientist in the field of biochemistry, biophysics, molecular medicine, biotechnology, pharmacology. Pharmaceutical companies which engage in R&D activities related to drug design.
- 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
- Edition: 1
- Volume: 206
- Published: May 30, 2024
- Imprint: Academic Press
- No. of pages: 528
- Language: English
- Hardback ISBN: 9780443293405
- eBook ISBN: 9780443293412
DT
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, USABD
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-IranVU
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 FloridaRead The Hidden World of Protein Aggregation on ScienceDirect