Abstract
The progressive production and subsequent accumulation of β-amyloid (Aβ), a proteolytic fragment of the membrane-associated amyloid precursor protein (APP), plays a central role in Alzheimers Disease (AD). Aβ is released in a soluble form that may be responsible for cognitive dysfunction in the early stages of the disease, then progressively forms oligomeric, multimeric and fibrillar aggregates, triggering neurodegeneration. Eventually, the aggregation and accumulation of Aβ culminates with the formation of extracellular plaques, one of the morphological hallmarks of the disease, detectable post-mortem in AD brains. In this review we report the known structural features of amyloid peptides and fibrils, and we give an overview of all small molecules that have been found to interact with Aβ aggregation. Deeper knowledge of the mechanism leading to amyloid fibrils along with their molecular structure and the molecular interactions responsible for activity of small molecules could supply useful information for the design of new AD therapeutic agents.
Keywords: β-amyloid, Alzheimer's disease, aggregation inhibitors
Current Medicinal Chemistry
Title: Beta Amyloid Aggregation Inhibitors: Small Molecules as Candidate Drugs for Therapy of Alzheimers Disease
Volume: 17 Issue: 27
Author(s): F. Re, C. Airoldi, C. Zona, M. Masserini, B. La Ferla, N. Quattrocchi and F. Nicotra
Affiliation:
Keywords: β-amyloid, Alzheimer's disease, aggregation inhibitors
Abstract: The progressive production and subsequent accumulation of β-amyloid (Aβ), a proteolytic fragment of the membrane-associated amyloid precursor protein (APP), plays a central role in Alzheimers Disease (AD). Aβ is released in a soluble form that may be responsible for cognitive dysfunction in the early stages of the disease, then progressively forms oligomeric, multimeric and fibrillar aggregates, triggering neurodegeneration. Eventually, the aggregation and accumulation of Aβ culminates with the formation of extracellular plaques, one of the morphological hallmarks of the disease, detectable post-mortem in AD brains. In this review we report the known structural features of amyloid peptides and fibrils, and we give an overview of all small molecules that have been found to interact with Aβ aggregation. Deeper knowledge of the mechanism leading to amyloid fibrils along with their molecular structure and the molecular interactions responsible for activity of small molecules could supply useful information for the design of new AD therapeutic agents.
Export Options
About this article
Cite this article as:
Re F., Airoldi C., Zona C., Masserini M., Ferla B. La, Quattrocchi N. and Nicotra F., Beta Amyloid Aggregation Inhibitors: Small Molecules as Candidate Drugs for Therapy of Alzheimers Disease, Current Medicinal Chemistry 2010; 17 (27) . https://dx.doi.org/10.2174/092986710791959729
DOI https://dx.doi.org/10.2174/092986710791959729 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
- 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
-
Tumor-Targeting Peptides and Small Molecules as Anti-Cancer Agents to Overcome Drug Resistance
Current Medicinal Chemistry Designing, Optimisation & Characterization of Sustained Release Matrix Pellets Prepared by Extrusion Spheronization Containing Mixture of Proteolytic Enzymes
Current Drug Delivery Polyamines in Gut Inflammation and Allergy
Current Medicinal Chemistry - Anti-Inflammatory & Anti-Allergy Agents The Pharmacological Treatment of Cachexia
Current Drug Targets Molecular Probes for Malignant Melanoma Imaging
Current Pharmaceutical Biotechnology The Role of Levomilnacipran in the Management of Major Depressive Disorder: A Comprehensive Review
Current Neuropharmacology Resveratrol and Lifespan in Model Organisms
Current Medicinal Chemistry Methods for Hydroxamic Acid Synthesis
Current Organic Chemistry Graphical Abstracts
Medicinal Chemistry Telemedicine, Genomics and Personalized Medicine: Synergies and Challenges
Current Pharmacogenomics and Personalized Medicine Effects of Molecular Hydrogen Assessed by an Animal Model and a Randomized Clinical Study on Mild Cognitive Impairment
Current Alzheimer Research Membrane Interactions of Oligomeric Alpha-Synuclein: Potential Role in Parkinsons Disease
Current Protein & Peptide Science Hypoxia-Inducible Factors and Sphingosine 1-Phosphate Signaling
Anti-Cancer Agents in Medicinal Chemistry Heat Shock Response Regulates Insulin Sensitivity and Glucose Homeostasis: Pathophysiological Impact and Therapeutic Potential
Current Diabetes Reviews Cyclooxygenase-1 and -2 in the Different Stages of Alzheimers Disease Pathology
Current Pharmaceutical Design Opioid Dependency and Myocardial Infarction: A Systematic Review and Meta-Analysis
Current Reviews in Clinical and Experimental Pharmacology Epi-Drugs and Epi-miRs: Moving Beyond Current Cancer Therapies
Current Cancer Drug Targets Impaired Spatial Memory after Ketamine Administration in Chronic Low Doses
Current Neuropharmacology Comparison of the Ability of Pyridinium Aldoximes to Reactivate Human RBC Cholinesterases Inhibited by Ethyl- and Methyl-Paraoxon
Current Organic Chemistry Receptor-Independent Effects of Endocannabinoids on Ion Channels
Current Pharmaceutical Design