Abstract
Amyloid beta peptide (Aβ) is recognised as a main feature of Alzheimer’s disease (AD). Increasing evidence suggests that small soluble oligomers of Aβ are the toxic form of the peptide and may instigate AD. Different factors including some key residues within Aβ molecule, the cell membrane, prion protein and metals play important roles in developing AD. Significant progress has been made to understand these factors and elucidate the mechanism of cytotoxicity of Aβ. This review summarizes recent findings in the area of Aβ and AD research, and this current knowledge could enable medicinal chemists to design and develop therapeutics to treat AD.
Keywords: Amyloid beta peptide, Alzheimer’s disease, oligomers, cytotoxicity, prion protein, metal interactions.
Current Medicinal Chemistry
Title:Amyloid Beta (Aβ) Peptide and Factors that Play Important Roles in Alzheimer’s Disease
Volume: 23 Issue: 9
Author(s): Elaheh Jamasbi, John D. Wade, Frances Separovic and Mohammed A. Hossain
Affiliation:
Keywords: Amyloid beta peptide, Alzheimer’s disease, oligomers, cytotoxicity, prion protein, metal interactions.
Abstract: Amyloid beta peptide (Aβ) is recognised as a main feature of Alzheimer’s disease (AD). Increasing evidence suggests that small soluble oligomers of Aβ are the toxic form of the peptide and may instigate AD. Different factors including some key residues within Aβ molecule, the cell membrane, prion protein and metals play important roles in developing AD. Significant progress has been made to understand these factors and elucidate the mechanism of cytotoxicity of Aβ. This review summarizes recent findings in the area of Aβ and AD research, and this current knowledge could enable medicinal chemists to design and develop therapeutics to treat AD.
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Cite this article as:
Jamasbi Elaheh, Wade D. John, Separovic Frances and Hossain A. Mohammed, Amyloid Beta (Aβ) Peptide and Factors that Play Important Roles in Alzheimer’s Disease, Current Medicinal Chemistry 2016; 23 (9) . https://dx.doi.org/10.2174/0929867323666160229113911
DOI https://dx.doi.org/10.2174/0929867323666160229113911 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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