Abstract
The process of protein misfolding and aggregation has been associated with an increasing number of pathological conditions that include Alzheimers and Parkinsons diseases, and type II diabetes. In addition, the discovery that proteins unrelated to any known disorder can be converted into aggregates of morphologies similar to those found in diseased tissue has lead to the recognition that this type of assemblies represents a generic state of polypeptide chains. Therefore, despite the enormous complexity of the in vivo mechanisms that have evolved in living organisms to prevent and control the formation of protein aggregates, the process of aggregation itself appears ultimately to be caused by intrinsic properties of polypeptide chains, in particular by the tendency of the backbone to form hydrogen bonds, and be modulated by the presence of specific patterns of hydrophobic and charged residues. Theoreticians have just recently started to respond to the challenge of identifying the determinants of the aggregation process. In this review, we provide an account of the theoretical results obtained so far.
Keywords: Protein misfolding, protein aggregation, amyloid fibrils, molecular dynamics, sensitive regions for aggregation, aggregation propensity, aggregation mechanism
Protein & Peptide Letters
Title: Theoretical Approaches to Protein Aggregation
Volume: 13 Issue: 3
Author(s): Joerg Gsponer and Michele Vendruscolo
Affiliation:
Keywords: Protein misfolding, protein aggregation, amyloid fibrils, molecular dynamics, sensitive regions for aggregation, aggregation propensity, aggregation mechanism
Abstract: The process of protein misfolding and aggregation has been associated with an increasing number of pathological conditions that include Alzheimers and Parkinsons diseases, and type II diabetes. In addition, the discovery that proteins unrelated to any known disorder can be converted into aggregates of morphologies similar to those found in diseased tissue has lead to the recognition that this type of assemblies represents a generic state of polypeptide chains. Therefore, despite the enormous complexity of the in vivo mechanisms that have evolved in living organisms to prevent and control the formation of protein aggregates, the process of aggregation itself appears ultimately to be caused by intrinsic properties of polypeptide chains, in particular by the tendency of the backbone to form hydrogen bonds, and be modulated by the presence of specific patterns of hydrophobic and charged residues. Theoreticians have just recently started to respond to the challenge of identifying the determinants of the aggregation process. In this review, we provide an account of the theoretical results obtained so far.
Export Options
About this article
Cite this article as:
Gsponer Joerg and Vendruscolo Michele, Theoretical Approaches to Protein Aggregation, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338407
DOI https://dx.doi.org/10.2174/092986606775338407 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
- 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
-
A Chronological Review of Potential Disease-Modifying Therapeutic Strategies for Alzheimer's Disease
Current Pharmaceutical Design Frontier View on Nanotechnological Strategies for Neuro-therapy
Current Drug Metabolism Induced Pluripotent Stem Cells and Their Potential for Basic and Clinical Sciences
Current Cardiology Reviews A Review on GABA/Glutamate Pathway for Therapeutic Intervention of ASD and ADHD
Current Medicinal Chemistry Emerging Perspectives on DNA Double-strand Breaks in Neurodegenerative Diseases
Current Neuropharmacology Mitochondrial Biogenesis: A Therapeutic Target for Neurodevelopmental Disorders and Neurodegenerative Diseases
Current Pharmaceutical Design Mitophagy in Neurodegeneration: An Opportunity for Therapy?
Current Drug Targets Meet Our Associate Editorial Board Member
Current Psychopharmacology Marine Sesterterpenes: An Overview
Current Organic Chemistry MicroRNAs Involved in Oxidative Stress Processes Regulating Physiological and Pathological Responses
MicroRNA Potential of Bone Marrow Stromal Cells in Applications for Neuro-Degenerative, Neuro-Traumatic and Muscle Degenerative Diseases
Current Neuropharmacology Pursuing Chemical Efficiency by Using Supported Organocatalysts for Asymmetric Reactions under Aqueous Conditions
Current Organocatalysis Group I Metabotropic Receptor Neuroprotection Requires Akt and Its Substrates that Govern FOXO3a, Bim, and β-Catenin During Oxidative Stress
Current Neurovascular Research Hypothalamic and Neuroendocrine Changes in Huntingtons Disease
Current Drug Targets Emerging and Alternative Therapies For Parkinson Disease: An Updated Review
Current Pharmaceutical Design Adenosine-to-Inosine RNA Editing: Perspectives and Predictions
Mini-Reviews in Medicinal Chemistry Volumetric Analysis of the Hypothalamus, Amygdala and Hippocampus in Non-Suicidal and Suicidal Mood Disorder Patients – A Post-Mortem Study
CNS & Neurological Disorders - Drug Targets Treatment Options in Alzheimer´s Disease: The GABA Story
Current Pharmaceutical Design GPCR Binding Technologies: An Overview
Current Topics in Medicinal Chemistry The Phosphoinositide Signal Transduction Pathway in the Pathogenesis of Alzheimer’s Disease
Current Alzheimer Research