![conference banner](/images/conference-banner.jpeg)
Abstract
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimers and Parkinsons diseases. Evidence that α-synuclein amyloidogenesis plays a causative role in the development of Parkinsons disease is furnished by a variety of genetic, neuropathological and biochemical studies. There is a major interest in understanding the structural and toxicity features of the various species populated along the aggregation pathway of this protein. The development of multidimensional Nuclear Magnetic Resonance (NMR) spectroscopy in liquid and solid state over the last decade has significantly increased the scope of molecules that are amenable for structural studies. The aim of this review is to provide a picture of how NMR tools were used in concert to decipher the structural and dynamic properties of the intrinsically disordered protein α- synuclein in its native, oligomeric, fibril and membrane-bound states. Understanding the structural and molecular basis behind the aggregation pathway of α-synuclein is key to advance in the design of a therapeutic strategy.
Keywords: Amyloid, intrinsically disordered proteins, NMR spectroscopy, Parkinson's disease, structural biology, Amyloid Aggregation, α-Synuclein, toxic conformation, Alzheimer's disease, Neurodegenerative Diseases, fibril morphology
Current Protein & Peptide Science
Title: Structures Behind the Amyloid Aggregation of α-Synuclein: An NMR based Approach
Volume: 12 Issue: 3
Author(s): Maria L. Orcellet and Claudio O. Fernandez
Affiliation:
Keywords: Amyloid, intrinsically disordered proteins, NMR spectroscopy, Parkinson's disease, structural biology, Amyloid Aggregation, α-Synuclein, toxic conformation, Alzheimer's disease, Neurodegenerative Diseases, fibril morphology
Abstract: The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimers and Parkinsons diseases. Evidence that α-synuclein amyloidogenesis plays a causative role in the development of Parkinsons disease is furnished by a variety of genetic, neuropathological and biochemical studies. There is a major interest in understanding the structural and toxicity features of the various species populated along the aggregation pathway of this protein. The development of multidimensional Nuclear Magnetic Resonance (NMR) spectroscopy in liquid and solid state over the last decade has significantly increased the scope of molecules that are amenable for structural studies. The aim of this review is to provide a picture of how NMR tools were used in concert to decipher the structural and dynamic properties of the intrinsically disordered protein α- synuclein in its native, oligomeric, fibril and membrane-bound states. Understanding the structural and molecular basis behind the aggregation pathway of α-synuclein is key to advance in the design of a therapeutic strategy.
Export Options
About this article
Cite this article as:
L. Orcellet Maria and O. Fernandez Claudio, Structures Behind the Amyloid Aggregation of α-Synuclein: An NMR based Approach, Current Protein & Peptide Science 2011; 12 (3) . https://dx.doi.org/10.2174/138920311795860160
DOI https://dx.doi.org/10.2174/138920311795860160 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
Call for Papers in Thematic Issues
Advancements in Proteomic and Peptidomic Approaches in Cancer Immunotherapy: Unveiling the Immune Microenvironment
The scope of this thematic issue centers on the integration of proteomic and peptidomic technologies into the field of cancer immunotherapy, with a particular emphasis on exploring the tumor immune microenvironment. This issue aims to gather contributions that illustrate the application of these advanced methodologies in unveiling the complex interplay ...read more
Artificial Intelligence for Protein Research
Protein research, essential for understanding biological processes and creating therapeutics, faces challenges due to the intricate nature of protein structures and functions. Traditional methods are limited in exploring the vast protein sequence space efficiently. Artificial intelligence (AI) and machine learning (ML) offer promising solutions by improving predictions and speeding up ...read more
Nutrition and Metabolism in Musculoskeletal Diseases
The musculoskeletal system consists mainly of cartilage, bone, muscles, tendons, connective tissue and ligaments. Balanced metabolism is of vital importance for the homeostasis of the musculoskeletal system. A series of musculoskeletal diseases (for example, sarcopenia, osteoporosis) are resulted from the dysregulated metabolism of the musculoskeletal system. Furthermore, metabolic diseases (such ...read more
Protein/protein and RNA/protein interactions are essential for molecular regulations
Protein-protein and RNA-protein interactions are fundamental to the intricate regulatory mechanisms that govern various cellular processes, playing a crucial role in maintaining the delicate balance and coordination within the complex molecular landscape. Proteins, the workhorses of the cell, engage in a myriad of interactions, both with other proteins and with ...read more
Related Journals
![Wayfinder Image](/images/wayfinder.jpg)
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Oxidative Stress and Antioxidant Potential of One Hundred Medicinal Plants
Current Topics in Medicinal Chemistry Novel Targets in Multiple Sclerosis: To Oxidative Stress and Beyond
Current Topics in Medicinal Chemistry A Review on Synthesis of Benzothiazole Derivatives
Current Organocatalysis Application of Stem Cell Therapy During the Treatment of HIV/AIDS and Duchenne Muscular Dystrophy
Current Stem Cell Research & Therapy Challenges in Neuronal Apoptosis
Current Alzheimer Research Investigating <i>Bacopa monnieri L.</i> Therapeutic Potential for the Treatment of Neurological Diseases
Current Pharmaceutical Design Tacrine Derivatives and Alzheimers Disease
Current Medicinal Chemistry Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology
Current Alzheimer Research Neuroprotective Effects of <i>Nardostachys jatamansi</i> Against BSO Induced Anxiety via its Antioxidant Machinery and by Elevating Catecholamines and GABA levels in Mice
Current Traditional Medicine Patent Selections
Recent Patents on Regenerative Medicine Resolution-Associated Molecular Patterns (RAMPs) as Endogenous Regulators of Glia Functions in Neuroinflammatory Disease
CNS & Neurological Disorders - Drug Targets Systemic Inflammation, Infection, ApoE Alleles, and Alzheimer Disease: A Position Paper
Current Alzheimer Research Functional Roles of Neuronal Nitric Oxide Synthase in Neurodegenerative Diseases and Mood Disorders
Current Alzheimer Research The Zebrafish Model as a New Discovery Path for Medicinal Plants in the Treatment of Parkinson’s Disease
CNS & Neurological Disorders - Drug Targets Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging
Current Molecular Pharmacology Purinergic Signaling and Energy Homeostasis in Psychiatric Disorders
Current Molecular Medicine Focus on the Role of Glutamate in the Pathology of the Peripheral Nervous System
CNS & Neurological Disorders - Drug Targets The Role of P-Glycoprotein in Psychiatric Disorders: A Reliable Guard of the Brain?
Central Nervous System Agents in Medicinal Chemistry Glaucoma and Alzheimer Disease: One Age-Related Neurodegenerative Disease of the Brain
Current Neuropharmacology Homocysteine in Neurology: From Endothelium to Neurodegeneration
Current Nutrition & Food Science