Abstract
Understanding the mechanisms by which amyloid fibrils are formed, both in vivo and in vitro, is vital for developing methods to treat and prevent debilitating deposition diseases such as Alzheimers disease, Parkinsonas disease, type II diabetes and systemic amyloidoses. In recent years, computer modelling and biophysical studies have broadened our understanding of the biochemical mechanisms underpinning protein aggregation. As a result, it is now believed that the ability to form fibrils is an intrinsic property of polypeptide chains and not isolated to disease-related proteins or peptides. Molecular chaperones are a diverse group of functionally related proteins well known for their ability to suppress amyloid formation, and are likely to be important determinants in deciding the fate of protein aggregation prone proteins in vivo. Evidence is presented that suggests that there is striking commonality in the anti-amyloidogenic activity of molecular chaperones regardless of their structural and spatial differences. In this review, we focus on what in vitro biophysical studies tell us about amyloid formation and molecular chaperones, and how investigating the role of chaperones in fibril formation can enhance our understanding of protein misfolding diseases.
Keywords: Amyloid, protein deposition disease, chaperone, oligomer, aggregation
Current Chemical Biology
Title: Protein Chemistry of Amyloid Fibrils and Chaperones: Implications for Amyloid Formation and Disease
Volume: 4 Issue: 2
Author(s): Justin J. Yerbury and Janet R. Kumita
Affiliation:
Keywords: Amyloid, protein deposition disease, chaperone, oligomer, aggregation
Abstract: Understanding the mechanisms by which amyloid fibrils are formed, both in vivo and in vitro, is vital for developing methods to treat and prevent debilitating deposition diseases such as Alzheimers disease, Parkinsonas disease, type II diabetes and systemic amyloidoses. In recent years, computer modelling and biophysical studies have broadened our understanding of the biochemical mechanisms underpinning protein aggregation. As a result, it is now believed that the ability to form fibrils is an intrinsic property of polypeptide chains and not isolated to disease-related proteins or peptides. Molecular chaperones are a diverse group of functionally related proteins well known for their ability to suppress amyloid formation, and are likely to be important determinants in deciding the fate of protein aggregation prone proteins in vivo. Evidence is presented that suggests that there is striking commonality in the anti-amyloidogenic activity of molecular chaperones regardless of their structural and spatial differences. In this review, we focus on what in vitro biophysical studies tell us about amyloid formation and molecular chaperones, and how investigating the role of chaperones in fibril formation can enhance our understanding of protein misfolding diseases.
Export Options
About this article
Cite this article as:
J. Yerbury Justin and R. Kumita Janet, Protein Chemistry of Amyloid Fibrils and Chaperones: Implications for Amyloid Formation and Disease, Current Chemical Biology 2010; 4 (2) . https://dx.doi.org/10.2174/2212796811004020089
DOI https://dx.doi.org/10.2174/2212796811004020089 |
Print ISSN 2212-7968 |
Publisher Name Bentham Science Publisher |
Online ISSN 1872-3136 |
- 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
- Announcements
Related Articles
-
Management of the Menopausal Disturbances and Oxidative Stress
Current Pharmaceutical Design A Direct Interaction Between Mitochondrial Proteins and Amyloid-β Peptide and its Significance for the Progression and Treatment of Alzheimer’s Disease
Current Medicinal Chemistry Inflammatory Caspases: Targets for Novel Therapies
Current Pharmaceutical Design Tianeptine: A Novel Atypical Antidepressant that May Provide New Insights into the Biomolecular Basis of Depression
Recent Patents on CNS Drug Discovery (Discontinued) Molecular, Cellular and Clinical Aspects of Intracerebral Hemorrhage: Are the Enemies Within?
Current Neuropharmacology Patent Annotations
Recent Patents on CNS Drug Discovery (Discontinued) Topical Delivery of Drugs for the Effective Treatment of Fungal Infections of Skin
Current Pharmaceutical Design Molecular Imaging of Stem Cell Transplantation for Neurodegenerative Diseases
Current Pharmaceutical Design Nitric Oxide, Epileptic Seizures, and Action of Antiepileptic Drugs
CNS & Neurological Disorders - Drug Targets Extranuclear Localization of SIRT1 and PGC-1α: An Insight into Possible Roles in Diseases Associated with Mitochondrial Dysfunction
Current Molecular Medicine Selenium and Clinical Trials: New Therapeutic Evidence for Multiple Diseases
Current Medicinal Chemistry Protein Cysteine Modifications: (1) Medicinal Chemistry for Proteomics
Current Medicinal Chemistry Intracellular Bioinorganic Chemistry and Cross Talk Among Different -Omics
Current Topics in Medicinal Chemistry Mast Cell – Glia Dialogue in Chronic Pain and Neuropathic Pain: Blood-Brain Barrier Implications
CNS & Neurological Disorders - Drug Targets The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases
Current Genomics Neurotransmitters and Microglial-Mediated Neuroinflammation
Current Protein & Peptide Science Gene and Cell Therapy for Prion Diseases
Infectious Disorders - Drug Targets Transient Cerebral Ischemia Leads to TGF-β2 Expression in Golgi Apparatus Organelles
Current Neurovascular Research Parkinson's Disease: A Role for the Immune System
Current Molecular Pharmacology Matrix Metalloproteinases: New Routes to the Use of MT1-MMP As A Therapeutic Target in Angiogenesis-Related Disease
Current Pharmaceutical Design