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Amyloid Fibrils

Amyloid Fibrils

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, normally used to...

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Updated: Jun 25, 2026

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Identification of Broad-Spectrum Inhibitors Targeting Multiple Amyloidogenic Proteins Using Functional Group-Based

Jiajun Huang^1,2, Chaohong Da¹, Shengrui Zhai¹

¹School of Biomedical Engineering and Technology, Tianjin Medical University, Tianjin, PR China.

Assay and Drug Development Technologies

|June 23, 2026

Summary

This summary is machine-generated.

Researchers identified key molecular features for developing pan-amyloid drugs that target multiple protein misfolding diseases. This approach aids in discovering new treatments for amyloidosis by focusing on common binding characteristics.

Keywords:

amyloidogenic proteins functional group-based pan-amyloid therapeutics virtual screening

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Area of Science:

Biochemistry
Pharmacology
Drug Discovery

Background:

Amyloidosis involves protein misfolding and aggregation into toxic fibrils.
A conserved fibril structure suggests pan-amyloid therapeutics targeting multiple proteins are feasible.

Purpose of the Study:

To identify small molecules that bind to multiple amyloidogenic proteins.
To validate a functional group-based screening approach for multitarget drug discovery.

Main Methods:

Screened 10,272 small molecules against four amyloidogenic proteins: amyloid β, serum amyloid A1, islet amyloid polypeptide, and transthyretin.
Identified five critical functional groups for high-affinity binding.
Performed functional group-based screening to find pan-amyloid binding compounds.

Main Results:

Five functional groups were identified as crucial for binding to all four target proteins.
A workflow for functional group-driven screening was validated.
Efficient identification of candidate pan-amyloid binding compounds was achieved.

Conclusions:

Functional group-based screening is effective for multitarget drug discovery in amyloidosis.
This strategy facilitates the development of novel pan-amyloid therapeutics.
Findings offer insights into targeting diverse amyloidogenic proteins simultaneously.