Amyloid-Beta and Alzheimer’s Disease

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: 28 February 2025 | Viewed by 4077

Special Issue Editors


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Guest Editor
The Institute of Prophylactic Pharmacology, Shinagawa, Tokyo 140-0001, Japan
Interests: Alzheimer's disease; amyloid-beta (Aβ); high-density lipoprotein; oxidative stress
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
1. Laboratory of Pharmacology, School of Medicine, Koch University, Nankoku 783-0047, Japan
2. O-Force Co., Ltd., 3454 Irino Kuroshio-cho, Hata-gun, Kochi 789-1931, Japan
Interests: Alzheimer's disease; amyloid-beta (Aβ); high-density lipoprotein; oxidative stress

Special Issue Information

Dear Colleagues,

Alzheimer's disease (AD) is the most common neurodegenerative disorder. The pathological proteins primarily associated with AD are amyloid-beta (Aβ) and tau. The "amyloid cascade hypothesis" is currently the most widely accepted molecular mechanism underlying AD pathogenesis. It suggests that an imbalance in the production and clearance of Aβ in the brains of AD patients results in Aβ deposition and the formation of neurotoxic Aβ oligomers. Therefore, understanding the mechanisms behind Aβ production and clearance is crucial for developing effective strategies to slow or halt the progression of AD.

Based on the theory that Aβ accumulation and aggregation in the brain contribute to AD's onset and progression, anti-Aβ monoclonal antibodies have been developed and tested in clinical trials. This success has strengthened the amyloid-β hypothesis, positioning amyloid as a central factor in Alzheimer's disease. However, the amyloid cascade alone no longer fully explains AD development. It is now well recognized that neuroinflammation plays a significant role in AD pathogenesis.

This Special Issue focuses on the importance of amyloid-β research in understanding Alzheimer's disease and developing therapeutic agents. Additionally, we will explore other potential mechanisms, such as neuroinflammation, with an emphasis on the role of microglia and astrocytes. By doing so, we aim to provide a comprehensive understanding of Alzheimer's disease.

Potential topics include, but are not limited to, the following:

  1. Aβ production and assembly.
  2. Aβ/oxidative stress-induced neurotoxicity.
  3. Interactions between Aβ and tau in AD.
  4. Clearance mechanisms of Aβ.
  5. Anti-amyloid monoclonal antibodies and amyloid-related imaging abnormalities.
  6. Role of microglia and astrocytes in AD.
  7. Aβ/microglial-mediated neuroinflammation.

We look forward to your contributions.

Dr. Fumiaki Ito
Prof. Dr. Toshifumi Akizawa
Guest Editors

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Keywords

  • Alzheimer's disease (AD)
  • amyloid-beta (Aβ)
  • neurotoxicity of Aβ
  • Tau protein
  • Aβ phagocytosis
  • Aβ clearance
  • autophagy–lysosome system
  • anti-Aβ monoclonal antibodies
  • neuroinflammation in AD
  • glial cells in AD

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Published Papers (3 papers)

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15 pages, 2943 KiB  
Article
An 11-mer Synthetic Peptide Suppressing Aggregation of Aβ25-35 and Resolving Its Aggregated Form Improves Test Performance in an Aβ25-35-Induced Alzheimer’s Mouse Model
by Rina Nakamura, Akira Matsuda, Youichirou Higashi, Yoshihiro Hayashi, Motomi Konishi, Motoaki Saito and Toshifumi Akizawa
Biomolecules 2024, 14(10), 1234; https://doi.org/10.3390/biom14101234 - 29 Sep 2024
Viewed by 856
Abstract
There is a high demand for the development of drugs against Alzheimer’s disease (AD), which is related to the misfolding and aggregation of Amyloid-β (Aβ), due to the increasing number of patients with AD. In our present study, we aimed to assess the [...] Read more.
There is a high demand for the development of drugs against Alzheimer’s disease (AD), which is related to the misfolding and aggregation of Amyloid-β (Aβ), due to the increasing number of patients with AD. In our present study, we aimed to assess the aggregation inhibitory effect of various synthetic YS-peptides on Aβ25-35 to identify an applicable peptide for clinical use for AD treatment and prevention. Suppression and aggregate resolution activities of YS-peptides against Aβ25-35 were evaluated using a Thioflavin T assay and scanning electron microscopy (SEM). Structure–activity relationship studies revealed that YS-RD11 (RETLVYLTHLD) and YS-RE16 (RETLVYLTHLDYDDTE) showed suppression and aggregate-resolution activities. The effect of YS-peptides on phagocytosis in microglial cells (BV-2 cells) demonstrated that YS-RD11 and YS-RE16 activated the phagocytic ability of microglia. In the Aβ25-35-induced AD mouse model, YS-RD11 prevented and improved the deficits in short-term memory. In conclusion, YS-RD11 is a suitable candidate therapeutic drug against AD and uses a strategy similar to that used for antibodies. Full article
(This article belongs to the Special Issue Amyloid-Beta and Alzheimer’s Disease)
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15 pages, 4253 KiB  
Article
SKGQA, a Peptide Derived from the ANA/BTG3 Protein, Cleaves Amyloid-β with Proteolytic Activity
by Yusuke Hatakawa, Rina Nakamura, Toshifumi Akizawa, Motomi Konishi, Akira Matsuda, Tomoyuki Oe, Motoaki Saito and Fumiaki Ito
Biomolecules 2024, 14(5), 586; https://doi.org/10.3390/biom14050586 - 15 May 2024
Cited by 1 | Viewed by 1105
Abstract
Despite the extensive research conducted on Alzheimer’s disease (AD) over the years, no effective drug for AD treatment has been found. Therefore, the development of new drugs for the treatment of AD is of the utmost importance. We recently reported the proteolytic activities [...] Read more.
Despite the extensive research conducted on Alzheimer’s disease (AD) over the years, no effective drug for AD treatment has been found. Therefore, the development of new drugs for the treatment of AD is of the utmost importance. We recently reported the proteolytic activities of JAL-TA9 (YKGSGFRMI) and ANA-TA9 (SKGQAYRMA), synthetic peptides of nine amino acids each, derived from the Box A region of Tob1 and ANA/BTG3 proteins, respectively. Furthermore, two components of ANA-TA9, ANA-YA4 (YRMI) at the C-terminus end and ANA-SA5 (SKGQA) at the N-terminus end of ANA-TA9, exhibited proteolytic activity against amyloid-β (Aβ) fragment peptides. In this study, we identified the active center of ANA-SA5 using AEBSF, a serine protease inhibitor, and a peptide in which the Ser residue of ANA-SA5 was replaced with Leu. In addition, we demonstrate the proteolytic activity of ANA-SA5 against the soluble form Aβ42 (a-Aβ42) and solid insoluble form s-Aβ42. Furthermore, ANA-SA5 was not cytotoxic to A549 cells. These results indicate that ANA-SA5 is a promising Catalytide and a potential candidate for the development of new peptide drugs targeting Aβ42 for AD treatment. Full article
(This article belongs to the Special Issue Amyloid-Beta and Alzheimer’s Disease)
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15 pages, 362 KiB  
Opinion
Upsetting the Balance: How Modifiable Risk Factors Contribute to the Progression of Alzheimer’s Disease
by Caitlin M. Carroll and Ruth M. Benca
Biomolecules 2024, 14(3), 274; https://doi.org/10.3390/biom14030274 - 24 Feb 2024
Cited by 1 | Viewed by 1860
Abstract
Alzheimer’s disease (AD) is a neurodegenerative disorder affecting nearly one in nine older adults in the US. This number is expected to grow exponentially, thereby increasing stress on caregivers and health systems. While some risk factors for developing AD are genetic, an estimated [...] Read more.
Alzheimer’s disease (AD) is a neurodegenerative disorder affecting nearly one in nine older adults in the US. This number is expected to grow exponentially, thereby increasing stress on caregivers and health systems. While some risk factors for developing AD are genetic, an estimated 1/3 of AD cases are attributed to lifestyle. Many of these risk factors emerge decades before clinical symptoms of AD are detected, and targeting them may offer more efficacious strategies for slowing or preventing disease progression. This review will focus on two common risk factors for AD, metabolic dysfunction and sleep impairments, and discuss potential mechanisms underlying their relationship to AD pathophysiology. Both sleep and metabolism can alter AD-related protein production and clearance, contributing to an imbalance that drives AD progression. Additionally, these risk factors have bidirectional relationships with AD, where the presence of AD-related pathology can further disrupt sleep and worsen metabolic functioning. Sleep and metabolism also appear to have a bidirectional relationship with each other, indirectly exacerbating AD pathophysiology. Understanding the mechanisms involved in these relationships is critical for identifying new strategies to slow the AD cascade. Full article
(This article belongs to the Special Issue Amyloid-Beta and Alzheimer’s Disease)
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