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Biomolecules
Special Issues
Targeting Protein Misfolding: From Alzheimer's Amyloids to Therapeutic Peptides
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Targeting Protein Misfolding: From Alzheimer's Amyloids to Therapeutic Peptides

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: 16 September 2026 | Viewed by 3776

Special Issue Editor

Dr. Dariusz Stępkowski

E-Mail Website
Guest Editor
Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland
Interests: Alzheimer’s disease; prion diseases; amyloidogenesis; inhibitors of amyloidogenesis; amyloid fibrils
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein misfolding accompanies many complex diseases, including Alzheimer’s disease, diabetes and prion diseases. Whether this process is at the center of the etiology of these diseases still remains an open question. Recently, the FDA approved monoclonal antibodies for use against β-amyloid species, showing a very moderate influence on the slowing of the course of Alzheimer’s disease. This observation suggests a multi-factorial etiology of this disease—where protein misfolding along with other processes contributes to neurodegeneration. Therefore, amyloidogenic events are still worth studying.

The mechanism of the misfolding of proteins into amyloids has been thoroughly studied. On the other hand, the dissolution of mature fibrils and neurotoxic oligomers has been studied much less. Monoclonal antibody therapy is very costly and unlikely to solve the problem of dementia and Alzheimer’s disease. For this Special Issue, in the quest for alternative solutions, supporting multi-factorial therapy, we welcome contributions dealing with the process of the dissolution of amyloid species, especially concerning β-amyloid, and those focusing on peptides called β-sheet breakers. Contributions on further topics are welcome. Both theoretical and experimental approaches as well as reviews are welcome.  

Dr. Dariusz Stępkowski
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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

  • amyloidogenesis
  • amyloidosis
  • amyloid fibrils
  • dissolution of amyloid fibrils
  • beta-sheet breakers
  • peptide inhibitors
  • small molecule inhibitors

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Published Papers (2 papers)

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Review

21 pages, 1137 KB  
Review
Tau and β-Amyloid Relevant Pathology as a Central Therapeutic Target in Alzheimer’s Disease
by Lidia Strużyńska, Kamil Adamiak and Marta Sidoryk-Węgrzynowicz
Biomolecules 2026, 16(4), 595; https://doi.org/10.3390/biom16040595 - 17 Apr 2026
Viewed by 897
Abstract
Alzheimer’s disease (AD) is the leading cause of dementia, responsible for approximately 60–70% of cases globally. AD is a gradually progressive neurodegenerative disorder that is characterized by widespread deposition of β-amyloid (Aβ) plaques, followed by aggregation of tau protein in the neocortex, neurodegeneration, [...] Read more.
Alzheimer’s disease (AD) is the leading cause of dementia, responsible for approximately 60–70% of cases globally. AD is a gradually progressive neurodegenerative disorder that is characterized by widespread deposition of β-amyloid (Aβ) plaques, followed by aggregation of tau protein in the neocortex, neurodegeneration, and cognitive decline. Within these complex pathological interactions, Aβ and tau proteins, together with astrogliosis, neuroinflammation, and other factors, play a key role in the development of clinical AD. Accumulating evidence indicates that the formation of protein oligomers, followed by their aggregation into pathological fibrils, constitutes an early and critical step in the pathogenesis of the disease. Specific pathological proteins are often treated as biomarkers of particular diseases because their presence, concentration, or altered structure reflects an underlying disease process. It is well established that the Aβ and tau proteins are the key hallmarks of AD, and their mutual interaction may significantly influence the pathology of the disease. Early diagnosis is crucial for maximizing the therapeutic benefits of currently available symptomatic treatments, which can alleviate symptoms and modestly delay clinical deterioration in patients with AD. This review highlights the mechanisms involved in protein-dependent neurodegeneration and describes both traditional and novel approaches for the cure of AD. The most important aspect of this publication is the integration of the two key proteins: Aβ and tau, and the resulting shift toward a new therapeutic approach. Full article
(This article belongs to the Special Issue Targeting Protein Misfolding: From Alzheimer's Amyloids to Therapeutic Peptides)
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23 pages, 1253 KB  
Review
Advances in Bioactive Compounds from Plants and Their Applications in Alzheimer’s Disease
by Steve Pavlov, Santosh Kumar Prajapati, Dhananjay Yadav, Andrea Marcano-Rodriguez, Hariom Yadav and Shalini Jain
Biomolecules 2026, 16(1), 7; https://doi.org/10.3390/biom16010007 - 19 Dec 2025
Cited by 2 | Viewed by 2436
Abstract
Alzheimer’s disease (AD), the leading cause of dementia worldwide, is characterized by progressive neuronal loss, amyloid-β (Aβ) aggregation, tau hyperphosphorylation, oxidative stress, neuroinflammation, cholinergic dysfunction, and gut–brain axis dysregulation. Despite advances in anti-amyloid therapeutics, current interventions provide only modest symptomatic relief and face [...] Read more.
Alzheimer’s disease (AD), the leading cause of dementia worldwide, is characterized by progressive neuronal loss, amyloid-β (Aβ) aggregation, tau hyperphosphorylation, oxidative stress, neuroinflammation, cholinergic dysfunction, and gut–brain axis dysregulation. Despite advances in anti-amyloid therapeutics, current interventions provide only modest symptomatic relief and face limitations in accessibility, cost, and long-term efficacy. Plant-derived bioactive compounds, rooted in traditional medicine systems such as Ayurveda and Traditional Chinese Medicine, have gained increasing attention as multi-target therapeutic agents due to their pleiotropic actions, relative safety, and ability to cross the blood–brain barrier. This review synthesizes mechanistic and translational evidence on major phytochemicals, including withanolides (Withania somnifera), curcumin (Curcuma longa), ginkgolides and bilobalide (Ginkgo biloba), bacosides (Bacopa monnieri), ginsenosides (Panax ginseng), crocin/safranal (Crocus sativus), epigallocatechin-3-gallate (Camellia sinensis), rosmarinic acid (Salvia officinalis, Melissa officinalis), and asiaticosides (Centella asiatica). These compounds exert neuroprotective effects by inhibiting Aβ aggregation, reducing tau phosphorylation, scavenging reactive oxygen species, attenuating NF-κB-mediated inflammation, modulating cholinergic signaling, enhancing synaptic plasticity via brain-derived neurotrophic factor/cAMP response element-binding protein (BDNF/CREB) activation, and regulating gut microbiota. Multi-target approach analyses underscore their synergistic potential in targeting interconnected AD pathways. However, translation remains hindered by poor oral bioavailability, rapid metabolism, and variability in clinical outcomes. Advances in delivery platforms, including liposomes, bilosomes, solid lipid nanoparticles, and nanostructured lipid carriers, are improving stability, blood–brain penetration, and therapeutic efficacy in preclinical models. Collectively, plant-derived phytochemicals serve as promising, affordable, and multi-modal candidates for reshaping AD management, bridging traditional knowledge with modern therapeutic innovation. Full article
(This article belongs to the Special Issue Targeting Protein Misfolding: From Alzheimer's Amyloids to Therapeutic Peptides)
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