Work

Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape

Year: 2010

Type: review

Abstract: 3.1.Polymorphic Backbone Organizations within and between Sheets in Amyloid Fibrils: Potential Combinations 4824 3.2.Polymorphism in the U-Turns in Amyloid Fibrils 4826 3.3.Polymorphism in Association of β-Sheet Oligomers 4826 4. Other Protein/Peptide Sequences Also Have Polymorphic Fibrils Structures 4827 5. Sequences and Physicochemical Properties That Can Affect Amyloid Fibril Architectures 4828 5.1.Hydrophobicity Can Increase Amyloid Polymorphism 4828 5.2.Charged Residues Require a Specific Match, thus Decreasing Amyloid Diversity 4829 5.3.Steric Zipper Could Increase or Decrease Amyloid Diversity 4830 6. Polymorphism in Metal-Binding Sites in Alzheimer Aβ Amyloid: Zn 2+ , Cu 2+ , Fe 3+ , and Al 3+ 4830 7. Polymorphism in Soluble Aβ Oligomers Leads to Different Mechanisms of Toxicity 4831 8.The Energy Landscape of Amyloidogenic Proteins and Their Assemblies Is Rugged 4832 9. Conclusions 4833 10.

Source: Chemical Reviews

DOI: 10.1021/cr900377t

Authors: Yifat Miller, Buyong Ma, Ruth Nussinov

Institutions: Tel Aviv University, Center for Cancer Research

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: U.S. Department of Health and Human Services, National Institute for Health and Care Research, National Institutes of Health, National Cancer Institute