Author: Patrick J. SalvesonPublisher:
ISBN:
Category :
Languages : en
Pages : 0
Book Description
Exploring and Controlling the Supramolecular Assembly of Amyloid-Forming Peptides and Proteins with Chemical Model Systems
Author: Patrick J. SalvesonProtein Self-Assembly
Author: Jennifer J. McManusPublisher: Humana
ISBN: 9781493996803
Category : Science
Languages : en
Pages : 266
Book Description
This volume explores experimental and computational approaches to measuring the most widely studied protein assemblies, including condensed liquid phases, aggregates, and crystals. The chapters in this book are organized into three parts: Part One looks at the techniques used to measure protein-protein interactions and equilibrium protein phases in dilute and concentrated protein solutions; Part Two describes methods to measure kinetics of aggregation and to characterize the assembled state; and Part Three details several different computational approaches that are currently used to help researchers understand protein self-assembly. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Thorough and cutting-edge, Protein Self-Assembly: Methods and Protocols is a valuable resource for researchers who are interested in learning more about this developing field.
Biophysics And Biochemistry Of Protein Aggregation: Experimental And Theoretical Studies On Folding, Misfolding, And Self-assembly Of Amyloidogenic Peptides
Author: Jian-min YuanPublisher: World Scientific
ISBN: 9813202394
Category : Science
Languages : en
Pages : 327
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.
The Assembly and Structure of Self-assembling Peptides
Author: Kyle MorrisPublisher:
ISBN:
Category :
Languages : en
Pages :
Book Description
Self-assembling molecules are central to a plethora of processes found in nature, biotechnology and even disease. The importance of the non-covalent interaction of monomers to the formation of fibrillar assemblies is evident in the repeated use of this mechanism throughout nature, from essential cellular processes such as the formation of the cytoskeleton to the production of silk. Further, it has been recognised in the last two decades that a self-assembly mechanism, that is the formation of amyloid, underpins the pathology of protein misfolding diseases; it is therefore essential to dissect these mechanisms. Despite recent technological and model system developments, self-assembling molecules remain challenging to investigate. Using combined structural and biophysical characterisations of penta- and hexa-peptide self-assembling model systems these investigations shed further light on the structure of amyloid-like fibrils. The elucidation of the structures of these fibrillar systems not only has implications for disease but also makes them well placed for consideration for biotechnological applications. In reflecting upon how cross-ß structural architectures can be organised in the fibrillar state, a molecular and supramolecular model of fibrils formed by a fragment of!-synuclein is reported. The fibrils are found to consist of a novel and elaborate cross-ß architecture that leads to a helical supramolecular assembly spanning length scales previously unobserved for such a system. Where self-assembly is a useful route to supramolecular structure formation, the use of low molecular weight gelator (LMWG) peptides to create fibrillar structures with defined material properties is also explored. The complex link between molecular structure, self-assembled architecture, fibril formation, fibril interaction and ultimately bulk material properties is described. It is found that the determinants of self-assembly are distinct from the determinants of gelation and so future LMWG design will have to consider both individually. This work presents methodological advances in the characterisation of self-assembled structures. The investigations presented here have relevance for disease related processes but also to the technological use of these systems as materials. Finally, this work emphasises the beauty of the extravagant, yet elegant connection between molecular interaction and supramolecular selfassembly.
Self-Assembling Peptide Systems in Biology, Medicine and Engineering
Author: A. AggeliPublisher: Springer Science & Business Media
ISBN: 0306468905
Category : Science
Languages : en
Pages : 364
Book Description
One ofthe major drivers in biological research is the establishment ofstructures and functions of the 50,000 or so proteins in our bodies. Each has a characteristic- dimensional structure, highly "ordered" yet "disordered"! This structure is essential for a protein's function and, significantly, it must be sustained in the competitive and complex environment of the living cell. It is now being recognised that when a cell loses control, proteins can se- assemble into more complex supermolecular structures such as the amyloid fibres and plaques associated with the pathogenesis of prion (CJD) or age-related (Alzheimer's) diseases. This is a pointer to the wider significance of the self-assembling properties of polypeptides. It has been long known that, in silk, polypeptides are assembled into- sheet structures which impart on the material its highly exploitable properties of flexibility combined with high tensile strength. But only now emerging is the recognition that peptides can Self-assemble into a wide variety of non-protein-like structures, including fibrils, fibres, tubules, sheets and monolayers. These are exciting observations and, more so, the potential for materials and medical exploitations is so wide ranging that over 80 scientists from Europe, USA, Japan and Israel. met 1-6 July 1999 in Crete, to discuss the wide-ranging implications of these novel developments. There was a spirit of excitement about the workshop indicative of an important new endeavor. The emerging perception is that of a new class of materials set to become commercially viable early in the 21st century.
Amyloid Proteins
Author: Einar M. SigurdssonPublisher: Springer Science & Business Media
ISBN: 1592598749
Category : Science
Languages : en
Pages : 390
Book Description
A proven collection of readily reproducible techniques for studying amyloid proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
Peptide Catalysts, including Catalytic Amyloids
Author: Publisher: Elsevier
ISBN: 0443236682
Category : Science
Languages : en
Pages : 550
Book Description
Peptide Catalysts, including Catalytic Amyloids, Volume 697 in this esteemed series, highlights new advances in the field, with this new volume presenting interesting topics on Screening of oxidative behaviors in catalytic amyloid assemblies, Catalytic amyloids derived for natural proteins, AFM-IR studies of catalytic amyloids, MD structural studies of catalytic amyloids, Characterization of crystalline, amyloid-like amino acid assemblies, Computational modeling of supramolecular peptide assemblies, and Assembly and activity of short prion-inspired peptides. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in Methods in Enzymology series - Updated release includes the latest information on Peptide Catalysts, including Catalytic Amyloids
Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease
Author: J. Robin HarrisPublisher: Springer Science & Business Media
ISBN: 9400754167
Category : Medical
Languages : en
Pages : 654
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.
Fibrous Proteins: Amyloids, Prions and Beta Proteins
Author: John M. SquirePublisher: Elsevier
ISBN: 0080468950
Category : Science
Languages : en
Pages : 329
Book Description
Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial. Fibrous proteins act as molecular scaffolds in cells providing the supporting structures of our skeletons, bones, tendons, cartilage, and skin. They define the mechanical properties of our internal hollow organs such as the intestines, heart, and blood vessels. This volume covers such topics as Beta-Structures in Fibrous Proteins; B-Silks: Enhancing and Controlling Aggregation; Beta-Rolls, Beta-Helices and Other Beta-Solenoid Proteins; Natural Triple B-Stranded Fibrous Folds; Structure, Function and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants; X-Ray Fiber and powder Diffraction of PRP Prion Peptides; From the Polymorphism of Amyloid Fibrils to Their Assembly Mechanism and Cytotoxicity; Structural Models of Amyloid-like Fibrils.
Amyloid Fibrils and Prefibrillar Aggregates
Author: Daniel Erik OtzenPublisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
Book Description
Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.