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Biomolecules
Special Issues
Effective Strategies for the Treatment of Alzheimer’s Disease
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Effective Strategies for the Treatment of Alzheimer’s Disease

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

Deadline for manuscript submissions: closed (20 December 2022) | Viewed by 4552

Special Issue Editors

Dr. Hyuck Jin Lee

E-Mail Website
Guest Editor
Department of Chemistry Education, Kongju National University, Kongju 32588, Chungcheongnamdo, Korea
Interests: neurodegenerative diseases; Alzheimer’s disease; metalloenzymes; enzyme kinetics
Dr. Gernot Riedel

E-Mail Website
Co-Guest Editor
School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, UK
Interests: cognition; neurodegeneration; Alzheimer; parkinson; dementia; acetylcholine; in vivo preclinical models
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Ben A. Bahr

E-Mail Website
Co-Guest Editor
William C. Friday Laboratory, Biotechnology Research and Training Center, University of North Carolina-Pembroke, Pembroke, NC 28372, USA
Interests: Alzheimer's disease; proteostasis

Special Issue Information

Dear Colleagues,

Alzheimer’s disease (AD) is the most common form of dementia. It has been reported that 47 million people suffer from the disease worldwide, and this number is expected to increase to 75 million by 2030. The significant hallmarks of AD are i) progressive cellular deterioration in the hippocampus and other cortical areas of the brain, ii) amyloid-β (Aβ42 peptide) oligomerization and aggregation, iii) hyperphosphorylated tau and the propagation of tau pathology, iv) multi-proteinopathy that compromises proteostasis, v) decreased neurotransmission among cholinergic, glutamatergic, and perhaps other neurons, vi) mis-compartmentalization of metal ions, and vii) oxidative stress. Based on these hallmarks, various causes of the disease have been proposed, including Aβ42 oligomers, pathogenic tau species, and proteostatic stress, and numerous studies have invented potential drugs. Further, the FDA recently approved a drug, Aducanumab, for treating AD by targeting Aβ. However, there is a critical need for effective pharmacological or non-pharmacological agents to slow or reverse the disease. This Special Issue of Biomolecules focuses on the development of effective strategies for treating AD.

Dr. Hyuck Jin Lee
Dr. Gernot Riedel
Prof. Dr. Ben A. Bahr
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • alzheimer's disease 
  • amyloid proteins 
  • amyloid-beta 
  • tau 
  • acetylcholinesterase (AChE)  
  • metal ions 
  • reactive
  • oxygen species (ROS)
  • neurodegeneration

Published Papers (2 papers)

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Research

18 pages, 2626 KiB  
Article
Multi-Targeting Intranasal Nanoformulation as a Therapeutic for Alzheimer’s Disease
by Oksana Fihurka, Yanhong Wang, Yuzhu Hong, Xiaoyang Lin, Ning Shen, Haiqiang Yang, Breanna Brown, Marcus Mommer, Tarek Zieneldien, Yitong Li, Janice Kim, Minghua Li, Jianfeng Cai, Qingyu Zhou and Chuanhai Cao
Biomolecules 2023, 13(2), 232; https://doi.org/10.3390/biom13020232 - 25 Jan 2023
Cited by 3 | Viewed by 1841
Abstract
Melatonin, insulin, and Δ9-tetrahydrocannabinol (THC) have been shown to reverse cognitive deficits and attenuate neuropathologies in transgenic mouse models of Alzheimer’s disease (AD) when used individually. Here, we evaluated the therapeutic properties of long-term intranasal treatment with a novel nanoformulation containing melatonin, insulin, [...] Read more.
Melatonin, insulin, and Δ9-tetrahydrocannabinol (THC) have been shown to reverse cognitive deficits and attenuate neuropathologies in transgenic mouse models of Alzheimer’s disease (AD) when used individually. Here, we evaluated the therapeutic properties of long-term intranasal treatment with a novel nanoformulation containing melatonin, insulin, and THC in aged APPswe/PS1ΔE9 (APP/PS1) mice, a transgenic model of AD. Transgenic mice at the age of 12 months were intranasally administered with a new nanoformulation containing melatonin, insulin, and THC at doses of 0.04, 0.008, and 0.02 mg/kg, respectively, once daily for 3 months. The spatial memory of the mice was assessed using the radial arm water maze (RAWM) test before and after drug treatment. Brain tissues were collected at the end of the treatment period for the assessment of Aβ load, tauopathy state, and markers of mitochondrial function. The RAWM test revealed that the treatment with the melatonin–insulin–THC (MIT) nasal spray improved the spatial learning memory of APP/PS1 mice significantly. Results of protein analyses of brain homogenates indicated that MIT treatment significantly decreased the tau phosphorylation implicated in tau toxicity (p < 0.05) and the expression of CKMT1 associated with mitochondrial dysfunction. Moreover, MIT significantly decreased the expression of two mitochondrial fusion-related proteins, Mfn2 and Opa1 (p < 0.01 for both), while increasing the expression of a mitophagy regulator, Parkin, suggesting a compensatory enhancement of mitophagy due to MIT-promoted mitochondrial fusion. In conclusion, this study was the first to demonstrate the ability of an MIT nanoformulation to improve spatial memory in AD mice through its multi-targeting effects on Aβ production, tau phosphorylation, and mitochondrial dynamics. Thus, MIT may be a safe and effective therapeutic for AD. Full article
(This article belongs to the Special Issue Effective Strategies for the Treatment of Alzheimer’s Disease)
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23 pages, 3275 KiB  
Article
Novel Hominid-Specific IAPP Isoforms: Potential Biomarkers of Early Alzheimer’s Disease and Inhibitors of Amyloid Formation
by Qing-Rong Liu, Min Zhu, Qinghua Chen, Maja Mustapic, Dimitrios Kapogiannis and Josephine M. Egan
Biomolecules 2023, 13(1), 167; https://doi.org/10.3390/biom13010167 - 13 Jan 2023
Viewed by 2063
Abstract
(1) Background and aims: Amyloidosis due to aggregation of amyloid-β (Aβ42) is a key pathogenic event in Alzheimer’s disease (AD), whereas aggregation of mature islet amyloid polypeptide (IAPP37) in human islets leads to β-cell dysfunction. The aim of this [...] Read more.
(1) Background and aims: Amyloidosis due to aggregation of amyloid-β (Aβ42) is a key pathogenic event in Alzheimer’s disease (AD), whereas aggregation of mature islet amyloid polypeptide (IAPP37) in human islets leads to β-cell dysfunction. The aim of this study is to uncover potential biomarkers that might additionally point to therapy for early AD patients. (2) Methods: We used bioinformatic approach to uncover novel IAPP isoforms and developed a quantitative selective reaction monitoring (SRM) proteomic assay to measure their peptide levels in human plasma and CSF from individuals with early AD and controls, as well as postmortem cerebrum of clinical confirmed AD and controls. We used Thioflavin T amyloid reporter assay to measure the IAPP isoform fibrillation propensity and anti-amyloid potential against aggregation of Aβ42 and IAPP37. (3) Results: We uncovered hominid-specific IAPP isoforms: hIAPPβ, which encodes an elongated propeptide, and hIAPPγ, which is processed to mature IAPP25 instead of IAPP37. We found that hIAPPβ was significantly reduced in the plasma of AD patients with the accuracy of 89%. We uncovered that IAPP25 and a GDNF derived DNSP11 were nonaggregating peptides that inhibited the aggregation of IAPP37 and Aβ42. (4) Conclusions: The novel peptides derived from hIAPP isoforms have potential to serve as blood-derived biomarkers for early AD and be developed as peptide based anti-amyloid medicine. Full article
(This article belongs to the Special Issue Effective Strategies for the Treatment of Alzheimer’s Disease)
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