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This thesis presents a method for reliably and robustly producing samples of amyloid-β (Aβ) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide’s nanomechanical, elastic, thermal or spectroscopical properties. Amyloid-β (Aβ) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of Aβ with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.
This thesis presents a method for reliably and robustly producing samples of amyloid-? (A?) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide’s nanomechanical, elastic, thermal or spectroscopical properties. Amyloid-? (A?) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of A? with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.
Amyloid b ab undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy , dynamic light scattering and other physical techniques. By imaging samples of Ab with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.
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
This volume presents readers with the latest techniques to study nanoimaging and nanoprobing in application to a broad range of biological systems. The chapters in this book are divided into five parts, and cover topics such as imaging and probing of biomacromolecules including high-speed imaging and probing with AFM; probing chromatin structure with magnetic tweezers; and fluorescence correlation spectroscopy on genomic DNA in living cells. 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. Cutting-edge and through, Nanoscale Imaging: Methods and Protocols is a valuable resource for anyone interested in learning more about this developing and expanding field.
Amyloidosis is a degenerative protein misfolding disorder that leads to the extracellular accumulation of amyloid deposits containing protein fibrils, heparan sulfate proteoglycans, glycoproteins and apolipoproteins. To date, at least 27 proteins have been identified as components of pathologic amyloid fibrils. In systemic forms of the disease, amyloid deposits can evade the immune system and expand throughout various tissues. As the deposits grow, tissue architecture is disrupted, leading to organ dysfunction and death. In the US, there are ~3500 newly diagnosed patients with amyloidosis annually. The deposition of light chains as amyloid (AL amyloidosis) is the most common form of visceral disease. The prognoses for patients varies (median survival for AL 12-40 months), but those with cardiac involvement have a considerably less favorable prognosis (~9 months median survival). Many researchers and physicians believe that early detection of amyloidosis could improve patient survival. The current gold standard for diagnosis involves histological examination of biopsy-derived tissue specimens. This method is invasive, subject to sampling error, and can be quite challenging. In an attempt to facilitate diagnosis, molecular imaging techniques using amyloid-reactive tracers have been developed such that a whole body, non-invasive “picture” of amyloid burden in patients may be established. There are several imaging agents used clinically world-wide, but each of these has limitations regarding its adoption in the US (i.e. 123[123]I-SAP is not FDA-approved and cannot image cardiac amyloid deposits, 124[124]I-11-1F4 only images ~60% of patients, and 99m[99m]Tc-labeled bone-seeking agents cannot image the most common forms of amyloid disease in patients). Given these limitations, there is an unmet clinical need for a facile method of quantitatively detecting whole body amyloid burden in patients. To this end, we have developed synthetic, pan-amyloid-reactive peptides for use as radiotracers by using SPECT/CT or PET/CT molecular imaging to non-invasively detect whole body amyloid load in patients. Through numerous preclinical experiments using ex vivo and transgenic murine models of amyloidosis, the structurally related peptides were found to have unique in vivo characteristics. Our findings suggest that, if further optimized, certain peptides could have clinical merit for the early detection of multiple types of amyloidosis.
Non-Destructive Material Characterization Methods provides readers with a trove of theoretical and practical insight into how to implement different non-destructive testing methods for effective material characterization. The book starts with an introduction to the field before moving right into a discussion of a wide range of techniques that can be immediately implemented. Various imaging and microscopy techniques are first covered, with step-by-step insights on characterization using a polarized microscope, an atomic force microscope, computed tomography, ultrasonography, magnetic resonance imaging, infrared tomography, and more. Each chapter includes case studies, applications, and recent developments. From there, elemental assay and mapping techniques are discussed, including Raman spectroscopy, UV spectroscopy, atomic absorption spectroscopy, neutron activation analysis, and various others. The book concludes with sections covering displacement measurement techniques, large-scale facility techniques, and methods involving multiscale analysis and advanced analysis. Provides an overview of a wide-range of NDT material characterization methods, strengths and weaknesses of these methods, when to apply them, and more Includes eddy current sensing and imaging, ultrasonic sensing and imaging, RF and THz imaging, internet and cloud-based methods, among many others Presents case studies, applications and other insights on putting these methods into practice
Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties. Provides practical examples of nanoimaging research from leading molecular biology, cell biology, protein chemistry, biotechnology, genetics, and pharmaceutical labs Includes over 200 color images to illustrate the power of various nanoimaging technologies Focuses on nanoimaging techniques applied to protein misfolding and aggregation in molecular medicine
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