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Alzheimer's Amyloid: Structure, Function, and Disease
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Alzheimer's Amyloid: Structure, Function, and Disease

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".

Deadline for manuscript submissions: closed (30 August 2023) | Viewed by 7378

Special Issue Editors

Dr. Adam Jarmuła

E-Mail Website
Guest Editor
Nencki Institute of Experimental Biology of the Polish Academy of Sciences, Warsaw, Poland
Interests: structural biology; computational biology; protein crystallography; molecular modeling; molecular docking; drug design; molecular dynamics
Special Issues, Collections and Topics in MDPI journals
Dr. Dariusz Stępkowski

E-Mail Website
Guest Editor
Nencki Institute of Experimental Biology of the Polish Academy of Sciences, Warsaw, Poland
Interests: Alzheimer’s disease; prion diseases; amyloidogenesis; inhibitors of amyloidogenesis; amyloid fibrils

Special Issue Information

Dear Colleagues,

Alzheimer’s disease (AD), a fatal neurodegenerative disease, has puzzled the scientific community for over a century. AD currently affects 50 million patients and is estimated to reach 152 million in 2050. The COVID-19 pandemic may have significantly increased these estimates according to an alarming report showing a hazard ratio of 1.69 for new-onset AD in older people as a late sequel of COVID-19.  This may substantially increase the already enormous burden on public health budgets, health care and older people and societies. Therefore, despite the controversial approval of an expensive therapy with aducanumab and expected approval of the use of monoclonal antibodies against β-amyloid, there is an urgent need to find cheap and effective small-molecule treatments for this disease. For this Special Issue, we welcome studies concerning inhibitors of β-amyloid aggregation into oligomers and mature fibrils as well as compounds dissolving mature fibrils. Computational studies docking new compounds to β-amyloid monomers, oligomers and fibrils and molecular dynamics experiments alone or preliminary to “wet” biochemistry leading to elucidation of the mechanism underlying the inhibition of aggregation or dissolution of fibrils are also encouraged.

Dr. Adam Jarmuła
Dr. Dariusz Stępkowski
Guest Editors

Manuscript Submission Information

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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. Life is an international peer-reviewed open access monthly journal published by MDPI.

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Keywords

  • Alzheimer’s disease
  • beta-amyloid
  • in silico studies
  • amyloidogenesis
  • inhibition of fibrillation
  • dissolution of amyloid fibrils

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Published Papers (2 papers)

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Research

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16 pages, 5764 KiB  
Article
Virtual Screening of a Marine Natural Product Database for In Silico Identification of a Potential Acetylcholinesterase Inhibitor
by Anushree Chandrashekhar Gade, Manikanta Murahari, Parasuraman Pavadai and Maushmi Shailesh Kumar
Life 2023, 13(6), 1298; https://doi.org/10.3390/life13061298 - 31 May 2023
Cited by 8 | Viewed by 2947
Abstract
Alzheimer’s disease is characterized by amyloid-beta aggregation and neurofibrillary tangles. Acetylcholinesterase (AChE) hydrolyses acetylcholine and induces amyloid-beta aggregation. Acetylcholinesterase inhibitors (AChEI) inhibit this aggregation by binding to AChE, making it a potential target for the treatment of AD. In this study, we have [...] Read more.
Alzheimer’s disease is characterized by amyloid-beta aggregation and neurofibrillary tangles. Acetylcholinesterase (AChE) hydrolyses acetylcholine and induces amyloid-beta aggregation. Acetylcholinesterase inhibitors (AChEI) inhibit this aggregation by binding to AChE, making it a potential target for the treatment of AD. In this study, we have focused on the identification of potent and safe AChEI from the Comprehensive Marine Natural Product Database (CMNPD) using computational tools. For the screening of CMNPD, a structure-based pharmacophore model was generated using a structure of AChE complexed with the co-crystallized ligand galantamine (PDB ID: 4EY6). The 330 molecules that passed through the pharmacophore filter were retrieved, their drug-likeness was determined, and they were then subjected to molecular docking studies. The top ten molecules were selected depending upon their docking score and were submitted for toxicity profiling. Based on these studies, molecule 64 (CMNPD8714) was found to be the safest and was subjected to molecular dynamics simulations and density functional theory calculations. This molecule showed stable hydrogen bonding and stacked interactions with TYR341, mediated through a water bridge. In silico results can be correlated with in vitro studies for checking its activity and safety in the future. Full article
(This article belongs to the Special Issue Alzheimer's Amyloid: Structure, Function, and Disease)
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Review

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28 pages, 7506 KiB  
Review
Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases
by Soumick Naskar and Nidhi Gour
Life 2023, 13(7), 1523; https://doi.org/10.3390/life13071523 - 7 Jul 2023
Cited by 6 | Viewed by 3558
Abstract
Amyloids were conventionally referred to as extracellular and intracellular accumulation of Aβ42 peptide, which causes the formation of plaques and neurofibrillary tangles inside the brain leading to the pathogenesis in Alzheimer’s disease. Subsequently, amyloid-like deposition was found in the etiology of prion diseases, [...] Read more.
Amyloids were conventionally referred to as extracellular and intracellular accumulation of Aβ42 peptide, which causes the formation of plaques and neurofibrillary tangles inside the brain leading to the pathogenesis in Alzheimer’s disease. Subsequently, amyloid-like deposition was found in the etiology of prion diseases, Parkinson’s disease, type II diabetes, and cancer, which was attributed to the aggregation of prion protein, α-Synuclein, islet amyloid polypeptide protein, and p53 protein, respectively. Hence, traditionally amyloids were considered aggregates formed exclusively by proteins or peptides. However, since the last decade, it has been discovered that other metabolites, like single amino acids, nucleobases, lipids, glucose derivatives, etc., have a propensity to form amyloid-like toxic assemblies. Several studies suggest direct implications of these metabolite assemblies in the patho-physiology of various inborn errors of metabolisms like phenylketonuria, tyrosinemia, cystinuria, and Gaucher’s disease, to name a few. In this review, we present a comprehensive literature overview that suggests amyloid-like structure formation as a common phenomenon for disease progression and pathogenesis in multiple syndromes. The review is devoted to providing readers with a broad knowledge of the structure, mode of formation, propagation, and transmission of different extracellular amyloids and their implications in the pathogenesis of diseases. We strongly believe a review on this topic is urgently required to create awareness about the understanding of the fundamental molecular mechanism behind the origin of diseases from an amyloid perspective and possibly look for a common therapeutic strategy for the treatment of these maladies by designing generic amyloid inhibitors. Full article
(This article belongs to the Special Issue Alzheimer's Amyloid: Structure, Function, and Disease)
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