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Your Position: Home > Pre-formed Fibrils (PFFs)--A Novel Approach to Modeling Neurodegeneration

Pre-formed Fibrils (PFFs)--A Novel Approach to Modeling Neurodegeneration

PFFs, A Novel Approach to Modeling Neurodegeneration
Pre-formed Fibrils (PFFs) Background
Schematic presentation of protein misfolding and aggregation
Schematic presentation of protein misfolding and aggregation

Protein aggregation is a major pathological feature of neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis (ALS), and Huntington's disease (HD). Under pathological conditions, Tau, Amyloid beta, alpha-synuclein, TDP-43, Huntingtin and other proteins integrate into a wide array of undesirable structures, ranging from oligomers and prefibrillar assemblies to highly ordered aggregates. The fibrillar structure represents a rapid growth phase of protein aggregation as these fibrils are “active” and rapidly recruit monomers for elongation. In additions, these fibrils randomly break into shorter fragments that could act as “seeds”, which transmits to other cells and independently recruits monomers to form novel fibrils. Pre-formed fibrils (PFFs) are in vitro formed active fibrils that have this "seeding" activity and are capable of continuously recruiting soluble endogenous pathological proteins to form aggregates and finally induce neurodegenerative pathologies.

The establishment of reliable disease models is crucial for discovering the pathological mechanisms, evaluating the efficacy of therapeutic interventions, and assessing the safety of drug candidates. Compared with traditional disease modeling approaches, PFFs induced pathology does not depend on gene editing, chemical or physical damage, and it can better mimic naturally occurring pathological states processes. Therefore, PFFs is a novel approach to modeling neurodegenerative diseases.

Pre-formed Fibrils (PFFs) Production and Validation

PFFs could be generated from monomers either by incubating at 37°C and shaking, or by heparin induction. Quality control and precise initial preparation are important for successful experiments. One important aspect of successful induction of PFFs is the use of high-quality monomer with high purity, high concentration and correct conformation. Meanwhile, since the application of PFFs is cellular and animal experiments, the control of endotoxin is also an important factor. In addition, prior to the use of PFFs, PFFs should become a length of 50 nm or shorter via ultrasound to ensure the recruiting activity of PFFs as well as to facilitate the endocytosis of PFFs.

The morphology and activity of PFFs could be verified by electron microscope and thioflavin T (ThT) fluorescence assay respectively. Successfully induced PFFs show fibril structure under electron microscope. ThT assay is a classic assay to detect β-sheet structures. PFFs acquire more and more β-sheet structures as they recruit monomers, and when ThT binds to the β-sheet structure, the fluorescence value increases, thus reflecting the activity of PFFs.

Pre-formed Fibrils (PFFs) Product

As the brand of ACROBiosystems that focused on neuroscience, Aneuro provides Tau-441 PFFs, alpha-synuclein PFFs, Amyloid beta PFFs, TDP-43 PFFs and SOD-1 PFFs, supporting and accelerating the establishment of reliable neurodegenerative models.

PFFs Product list

More PFFs relevant products under development. PFFs are under development.
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PFFs Product Features

Produced by high-quality monomers: the purity and homogeneity of monomer is >95% as verified by MALS, more conducive to the formation of PFFs and ensure the activity.
Lower endotoxin: monomer endotoxin ≤ 1.0 EU/μg, suitable for various in vitro and in vivo experiments.
The aggregation morphology and recruitment activity of PFFs are verified by electron microscopy and ThT fluorescence assay. Free protocols are shared.
Customized products and services provided with a variety of fluorescent labeling solutions: Star Staining, Biotin labeling, chemical labeling, etc.
Stable lead time, strict control to ensure high batch-to-batch consistency, highly cost-effective.

PFFs Product Verification Data

PFFs morphology (electron microscopy)
As shown in the figure below, the Tau-441 PFFs have distinct fibrous structures under electron microscopy, demonstrating that our Tau-441 PFFs products have accurate morphology.
TEM of Human Tau-441/2N4R Pre-formed Fibrils Protein

TEM of Human Tau-441/2N4R Pre-formed Fibrils Protein (Cat. No. TAU-H5115).

PFFs Activity (ThT assay)
PFFs induced faster aggregation of Tau proteins than that of the control group with only monomer added.
PFFs Activity Verification (ThT assay)

Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) over time when tau wild-type monomers (Cat. No. TAU-H5117) are combined with tau wild-type Pre-formed Fibrils (Cat. No. TAU-H5115).


  • 1. Stroo E, Koopman M, Nollen EA, Mata-Cabana A. Cellular Regulation of Amyloid Formation in Aging and Disease. Front Neurosci (2017). doi: 10.3389/fnins.2017.00064. PMID: 28261044; PMCID: PMC5306383.

  • 2. Guo JL, Lee VM. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem (2011). doi: 10.1074/jbc.M110.209296. Epub 2011 Mar 3. PMID: 21372138; PMCID: PMC3083182.

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