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![Statistical Physics of Folding and Aggregation of Amyloid [beta]-protein of Alzheimer's Disease PDF](https://books.google.com/books/content/images/frontcover/kte7PgAACAAJ?fife=w150-h200)
Author: Sijung Yun
Publisher:
ISBN: 9781109927405
Category :
Languages : en
Pages : 86
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Book Description
We use a discrete molecular dynamics simulation method to study aggregation of Abeta40 and Abeta42. Our simulations with hydrophobic and hydrophilic interactions show the distributions of Abeta40 and Abeta42 aggregates are significantly different, in agreement with the experimental results. We show that the difference between Abeta40 and Abeta42 occurs already at the folding stage. Abeta42 folded structure is characterized by a turn in the C-terminus that is not present in Abeta40. We show that the amino acids in the same C-terminal region are also responsible for the strongest intermolecular contacts in Abeta42 aggregates, but not in Abeta40 aggregates.
![Statistical Physics of Folding and Aggregation of Amyloid [beta]-protein of Alzheimer's Disease PDF](https://books.google.com/books/content/images/frontcover/kte7PgAACAAJ?fife=w80-h100)
Author: Sijung Yun
Publisher:
ISBN: 9781109927405
Category :
Languages : en
Pages : 86
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Book Description
We use a discrete molecular dynamics simulation method to study aggregation of Abeta40 and Abeta42. Our simulations with hydrophobic and hydrophilic interactions show the distributions of Abeta40 and Abeta42 aggregates are significantly different, in agreement with the experimental results. We show that the difference between Abeta40 and Abeta42 occurs already at the folding stage. Abeta42 folded structure is characterized by a turn in the C-terminus that is not present in Abeta40. We show that the amino acids in the same C-terminal region are also responsible for the strongest intermolecular contacts in Abeta42 aggregates, but not in Abeta40 aggregates.
Author: Jian-min Yuan
Publisher: World Scientific
ISBN: 9813202394
Category : Science
Languages : en
Pages : 327
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Book Description
This book reviews current research on the important processes involved in neurodegenerative diseases (e.g. Alzheimer's disease) and the peptides and proteins involved in the amyloidogenic processes. It covers the design and developments of anti-amyloid inhibitors, and gives readers a fundamental understanding of the underlying oligomerization and aggregation processes of these diseases from both computational and experimental points of view.
Author:
Publisher: Elsevier
ISBN: 0443293414
Category : Science
Languages : en
Pages : 530
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Book Description
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. 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
Author: Sara Maria Ayala Mariscal
Publisher:
ISBN:
Category :
Languages : en
Pages : 132
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Book Description
Alzheimer's disease is the most frequent type of dementia. With an exponentially growing number of cases, understanding the underlying molecular events leading to this devastating condition is of crucial importance. Much evidence points to a disequilibrium in the production and degradation of amyloid beta (Aß), a normally physiological 42 amino acid peptide, as an early key event in Alzheimer's etiology. Whether Aß is overproduced or poorly degraded, the overall result is an abnormally large pool of peptide that gradually aggregates forming extracellular deposits of fibrils, called amyloid plaques, in specific brain regions. Hence, modulation of Aß aggregation process is one of the suggested approaches to control the evolution of Alzheimer's disease. Universally conserved molecular chaperones have been intensively studied for their capacity to prevent aggregation of disease-related proteins, and many of them have proven to efficiently modulate Alzheimer's Aß aggregation. In a scenario where chaperones are overexpressed or directly administered into the affected tissue, the universal conservation and the relatively poor client-specificity of generic chaperones can become a downside because of the risk of interaction with proteins other than the targeted one is not dismissible, and thus the consequences unpredictable. In the first part of this work, we looked upon a bacterial chaperone call SecB with an unusually robust holdase activity (i.e. it prevents early protein folding) as a promising modulator of Alzheimer's Aß peptide aggregation. [...].
Author: J. Robin Harris
Publisher: Springer Science & Business Media
ISBN: 9400754167
Category : Medical
Languages : en
Pages : 654
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Book Description
This volume of the Subcellular Biochemistry series is the result of the long-standing research interest of the editor in the molecular mechanism underlying Alzheimer’s disease and other amyloid diseases, indicated also by the earlier book in the series (Volume 38), devoted to Alzheimer’s disease. The broad coverage within the present amyloidogenesis book represents an attempt to collate current knowledge relating to the proteins and peptides involved in most of the known amyloid diseases, together with some amyloid/fibril-forming proteins and peptides that are not involved in diseases. Thus, the range of topics included is comprehensive and furthermore it was thought appropriate to include both basic science and clinical presentation of the subjects under discussion.
Author:
Publisher: Elsevier
ISBN: 0080468977
Category : Science
Languages : en
Pages : 412
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Book Description
The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part B (volume 412) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies. Presents detailed protocols Includes troubleshooting tips Provides coverage on structural biology, computational methods, and biology
Author: Todd Jonathan Gibson
Publisher:
ISBN:
Category :
Languages : en
Pages : 194
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Book Description
Author: J. Robin Harris
Publisher: Springer Science & Business Media
ISBN: 9780387232256
Category : Science
Languages : en
Pages : 442
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Book Description
To understand Alzheimer's disease (AD) is one of the major thrusts of present-day clinical research, strongly supported by more fimdamental cellular, biochemical, immunological and structural studies. It is these latter that receive attention within this book. This compilation of 20 chapters indicates the diversity of work currently in progress and summarizes the current state of knowledge. Experienced authors who are scientifically active in their fields of study have been selected as contributors to this book, in an attempt to present a reasonably complete survey of the field. Inevitably, some exciting topics for one reason or another have not been included, for which we can only apologize. Standardization of terminology is often a problem in science, not least in the Alzheimer field; editorial effort has been made to achieve standardization between the Chapters, but some minor yet acceptable personal / author variation is still present, i. e. P-amyloid/amyloid-P; Ap42/Apl-42/APi. 42! The book commences with a broad survey of the contribution that the range of available microscopical techniques has made to the study of Alzheimer's amyloid plaques and amyloid fibrillogenesis. This chapter also serves as an Introduction to the book, since several of the topics introduced here are expanded upon in later chapters. Also, it is significant to the presence of this chapter that the initial discovery of brain plaques, by Alois Alzheimer, utilized light microscopy, a technique that continues to be extremely valuable in present-day AD research.
![In Silico Study of Amyloid [beta]-protein Folding Relevant to Alzheimer's Disease PDF](https://books.google.com/books/content/images/frontcover/77_JSAAACAAJ?fife=w80-h100)
Author: Alfonso Ramon Lam Ng
Publisher:
ISBN:
Category :
Languages : en
Pages : 204
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Book Description
Author: Pier Luigi San Biagio
Publisher:
ISBN: 9788178953540
Category : Amyloidosis
Languages : en
Pages : 267
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Book Description
This book collects papers by biology, chemistry and physics researchers all actively working in the field of protein aggregation as related to amyloid diseases. Protein precipitates having a highly ordered, fibril-like structure accompany several fatal diseases, such as Alzheimer's, Parkinson's, Creutzfeldt-Jacob and Huntington diseases. Amyloid fibrils associated to different diseases share a common cross beta repeat structure, despite the lack of sequence homologies and structure similarities in the relative proteins. About 20 proteins are known to form amyloid fibrils under physiological conditions. In any of them a conformational change into an unfolding intermediate seems to be responsible for amyloid fibrils formation. A growing body of evidence indicates that in vitro any protein or polypeptide can assembly into fibrillar structures under mildly denaturing conditions, where metastable unfolding intermediates become stabilized. These findings have added further interest to the outstanding problem of protein folding/unfolding and aggregation, whose high interdisciplinary character touches upon biology, chemistry and physics. Indeed, only by joining different expertise we may hope to achieve a unifying view of protein aggregation mechanism in terms of a few general principles. A central issue in the problem of amyloid formation is the understanding of the thermodynamic transitions governing this type of self-organization process in which the symmetry of the interacting molecules should play a relevant role. The first paper of this volume by Manno deals with the modeling of amyloid formation in the frame of physics of colloidal coagulation, and highlights those theoretical aspects that can be investigated by experiments in vitro. The relevance of crowding and confinement, or a combination of them, on the aggregation of proteins in living system is discussed in the paper of Temussi, where results obtained from studies in vitro and in vivo are revised and compared. The paper by Higuchi et al. addresses the theme of disease transmission in living organisms. The authors present the case of systemic amyloidosis in mice showing that pre-formed amyloid fibrils injected in, or ingested by, mice susceptible to infection are capable to accelerate amyloid deposition. A new emerging hypothesis on the onset of amyloid diseases points out the role played by small oligomeric species representing early pre-fibrillar intermediates. Such small aggregates have been observed in the case of beta-peptide responsible for Alzheimer disease. The paper by Di Carlo et al. describes the toxic properties of beta-peptide aggregates with different size, and indicates the possible degeneration pathways leading to the disease. If pre-fibrillar small oligomers are amyloid intermediates, inhibiting their formation should be an important target for therapeutic strategies. The paper by Sgarbossa et al. illustrates the potential use of small polycyclic aromatic molecules that can act as fibrillogenesis inhibitors by imposing unfavorable conformational constraints to the aggregating molecules. The paper by Pastore discusses the aggregation properties of proteins having homo-polymeric stretches, whose tract length determines the onset of the pathologies. The most famous of them is the Huntington disease associated to expansion of polyglutamine repeat. Bisaglia et al. revised the case of alpha-synuclein involved in Parkinson disease. The paper describes the capacity of this protein of adopting different conformations as a response to the environments, with relation to its physiological function or possible pathological role. Finally, two papers concern the role of metal ions on protein aggregation. The paper by Morante gives a review of the possible harmful or useful effects of some metal ions on two pathological proteins, examined through the synergic use of computational and experimental techniques. The paper by Militello et al. describes metal effects on the conformational change and structural properties of aggregates of beta-lactoglobulin and bovine serum albumin, taken as convenient model systems for studying protein aggregation. We thank the contributing authors for having provide altogether a wide perspective, multi-faceted survey of the conceptual and experimental tools that can be applied for unraveling the mechanism of protein aggregation.
