Bio-nanoimaging, 1st Edition

  • Published By:
  • ISBN-10: 0123978211
  • ISBN-13: 9780123978219
  • DDC: 572.6
  • Grade Level Range: College Freshman - College Senior
  • 552 Pages | eBook
  • Original Copyright 2013 | Published/Released May 2014
  • This publication's content originally published in print form: 2013

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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.

Table of Contents

Front Cover.
Half Title Page.
Title Page.
Copyright Page.
1: Molecular Mechanisms of Protein Misfolding.
2: Nanoimaging and Nanotechnology of Aggregating Proteins: A. In Vitro Approaches.
3: Amyloid Fibril Length Quantification by Atomic Force Microscopy.
4: Imaging Nucleation, Growth and Heterogeneity in Self-Assembled Amyloid Phases.
5: Molecular-Level Insights into Amyloid Polymorphism from Solid-State Nuclear Magnetic Resonance.
6: Single-Molecule Imaging of Amyloid-β Protein (Aβ) of Alzheimer’s Disease: From Single-Molecule Structures to Aggregation Mechanisms and Membrane Interactions.
7: Nanomechanics of Neurotoxic Proteins: Insights at the Start of the Neurodegeneration Cascade.
8: Reporters of Amyloid Structural Polymorphism.
9: Conformation-Dependent Antibodies as Tools for Characterization of Amyloid Protein Aggregates.
10: Nanoimaging and Nanotechnology of Aggregating Proteins: B. In Vivo Approaches.
11: Analyzing Alzheimer’s Disease-Related Protein Deposition In Vivo By Multiphoton Laser Scanning Microscopy.
12: Probing Amyloid Aggregation and Morphology In Situ by Multiparameter Imaging and Super-Resolution Fluorescence Microscopy.
13: Imaging of Amyloid-β Aggregation Using a Novel Quantum dot Nanoprobe and its Advanced Applications.
14: Studying the Molecular Determinants of Protein Oligomerization in Neurodegenerative Disorders by Bimolecular Fluorescence Complementation.
15: Structure-Specific Intrinsic Fluorescence of Protein Amyloids Used to Study their Kinetics of Aggregation.
16: Real-Time Monitoring of Inclusion Formation in Living Zebrafish.
17: Scanning for Intensely Fluorescent Targets (SIFT) in the Study of Protein Aggregation at the Single-Particle Level.
18: Polymorphism of Protein Misfolding and Aggregated Species.
19: The Molecular Basis For TGFBIp-Related Corneal Dystrophies.
20: Aβ Fibril Polymorphism and Alzheimer’s Disease.
21: Structural Heterogeneity and Bioimaging of S100 Amyloid Assemblies.
22: Polymorphism of Tau Fibrils.
23: Amyloid-Like Protofibrils with Different Physical Properties.
24: Insulin Oligomers: Detection, Characterization and Quantification Using Different Analytical Methods.
25: Imaging the Morphology and Structure of Apolipoprotein Amyloid Fibrils.
26: Polymorphism of Amyloid Fibrils and their Complexes with Catalase.
27: On Possible Function and Toxicity of Multiple Oligomeric/Conformational States of a Globular Protein – Human Stefin B.
28: Fibrillar Structures of Yeast Prion Sup35 In Vivo.
29: Glycosaminoglycans and Fibrillar Polymorphism.
30: Dopamine-Induced α-Synuclein Oligomers.
31: The Formation of Amyloid-Like Superstructures: On the Growth of Amyloid Spherulites.
32: Characterizing Nanoscale Morphologic and Mechanical Properties of α-Synuclein Amyloid Fibrils with Atomic Force Microscopy.
33: Polymorphism in Casein Protein Aggregation and Amyloid Fibril Formation.
34: Structural Basis for the Polymorphism of β-Lactoglobulin Amyloid-Like Fibrils.
35: Fibrillation and Polymorphism of Human Serum Albumin.
36: Formation of α-Helix-Based Twisted Ribbon-Like Fibrils from Ionic-Complementary Peptides.
37: Polymorphism, Metastable Species and Interconversion: The Many States of Glucagon Fibrils.
38: Polymorphism of Protein Misfolding and Aggregation Processes.
39: Multiple Pathways of Lysozyme Aggregation.
40: Structure–Function Studies of Amyloid Pores in Alzheimer’s Disease as a Case Example of Neurodegenerative Diseases.
41: Nanoscale Optical Imaging of Protein Amyloids.
42: Assembly of Amyloid β-Protein Variants Containing Familial Alzheimer’s Disease-Linked Amino Acid Substitutions.
43: Role of Aberrant α-Synuclein–Membrane Interactions in Parkinson’s Disease.
44: ELOA – Equine Lysozyme Complexes with Oleic Acid: Structure and Cytotoxicity Studied by Bio-Imaging Techniques.
45: Structure of a Misfolded Intermediate of a PDZ Domain.
46: Intranuclear Amyloid – Local and Quantitative Analysis of Protein Fibrillation in the Cell Nucleus.
47: Conversion of α-Helical Proteins into an Alternative β-Amyloid Fibril Conformation.
48: The Effect of Shear Flow on Amyloid Fibril Formation and Morphology.
Subject Index.
Name Index.