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Related Concept Videos

Alzheimer's Disease: Treatment01:22

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Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Related Experiment Video

Updated: Mar 29, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Tau Protein Aggregation Inhibitors-Therapeutic Strategy for Concurrent Tau and Amyloid Aggregation Inhibition.

Thomas Gabriel Schreiner1,2, Romeo Cristian Ciobanu3, Oliver Daniel Schreiner1,4

  • 1Department of Medical Specialties III, Faculty of Medicine, "Grigore T. Popa" University of Medicine and Pharmacy, 700115 Iasi, Romania.

Biomedicines
|March 28, 2026
PubMed
Summary

This review explores tau protein aggregation inhibitors for neurodegenerative diseases like Alzheimer's. It highlights current drugs and novel compounds targeting both tau and amyloid-β pathologies for future therapies.

Keywords:
Alzheimer’s diseasecurcuminneurodegenerationsmall-molecule inhibitortau protein

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Area of Science:

  • Neuroscience
  • Pharmacology
  • Biochemistry

Background:

  • Tau protein aggregation into neurofibrillary tangles is central to neurodegenerative diseases, notably Alzheimer's disease.
  • Pathological tau disrupts neuronal function, promoting neuroinflammation and amyloid plaque formation, ultimately causing cell death.
  • Inhibiting tau aggregation is a critical therapeutic strategy for these debilitating conditions.

Purpose of the Study:

  • To provide a practical overview of current tau protein aggregation inhibitors.
  • To discuss emerging compounds with dual activity against tau and amyloid-β pathology.
  • To offer a forward-looking framework for developing next-generation disease-modifying therapies.

Main Methods:

  • Systematic analysis of recent preclinical and clinical evidence on tau aggregation inhibitors.
  • Review of small-molecule inhibitors and natural compounds targeting tau pathology.
  • Emphasis on compounds with dual activity against tau and amyloid-β.

Main Results:

  • Established classes of tau aggregation inhibitors are presented with examples from clinical trials.
  • Emerging compounds with dual tau and amyloid-β inhibitory activity are highlighted.
  • Mechanistic convergence, repurposing opportunities, and therapeutic combinations are discussed.

Conclusions:

  • Tau aggregation inhibitors represent a key research direction for neurodegenerative diseases.
  • Dual-acting compounds offer promising therapeutic potential for multifactorial diseases.
  • This review identifies promising candidates for future disease-modifying therapies.