our science

sFIDA is a platform technology for quantitation and sizing of single protein aggregates at unprecedented levels of sensitivity and specificity.

Surface-based Fluorescence Distribution Analysis

The sFIDA platform technology offers a cutting-edge approach for the quantitative detection of single oligomers and aggregates, which serve as biomarkers of central nervous system (CNS) diseases such as Alzheimer’s Disease (AD) and Parkinson’s Disease (PD). This platform integrates the precision of selective immunoassays with the superior sensitivity of fluorescence microscopy to count single particles. As a result, sFIDA can detect these biomarkers at unprecedented levels of sensitivity and specificity.

The versatility of the sFIDA platform is further highlighted by its successful application to a range of conditions and biological material, including brain homogenate, cerebrospinal fluid, blood plasma, and even stool samples. This broad applicability enables the use of sFIDA technology in diverse clinical and research settings, allowing for a more comprehensive understanding of the molecular basis of neurodegenerative disorders.

How it works

❶ Wells are chemically modified to bind a capture antibody and sample is added.

❷ Both, oligomers and monomers are bound by the capture antibody.

❸ Using the same epitope for capture and detection, only oligomers are probed – but no monomers.

❹ Individual oligomers are detected and counted by highly sensitive fluorescence microscopy.

In addition, the sFIDA platform holds significant promise for advancing drug development. By providing valuable insights into the pathogenesis of CNS diseases and the molecular underpinnings of neurodegenerative disorders, sFIDA technology can aid in the identification of novel therapeutic targets and the evaluation of drug efficacy.

The sFIDA platform technology was developed at the Forschungszentrum Jülich, a leading research institute in Germany. Since 2018, the technology is commercialized by the spin-off company attyloid GmbH, which is dedicated to providing innovative solutions for the detection and analysis of biomarkers associated with neurodegenerative diseases.

attyloid is more than 
a biotech company.

We are an academicy spin-off dedicated to the scientific rigor that the complex fields of protein misfolding and CNS diseases demand. Our research plays a critical role in diagnosing and understanding these diseases and paving the way for innovative therapeutics.

Peer-reviewed publications

At attyloid, we value the importance of peer-reviewed research. Our work has been published in reputable scientific journals, giving us a solid footing in the field of protein misfolding and aggregation. Our proprietary sFIDA technology platform sets us apart. Its ultra-sensitive quantitative capabilities have been rigorously examined and validated through peer-reviewed research, ensuring unparalleled accuracy and reliability.

  • Blood-based quantification of Aβ oligomers indicates impaired clearance from brain in ApoE ε4 positive subjects.

    Blömeke, L. et al.

    Commun Med 4:262 (2024).

  • Elevated Aβ aggregates in feces from Alzheimer’s disease patients: a proof-of-concept study

    Pils, M. et al.

    Alzheimers Res Therapy 16:223 (2024).

  • IAPP – oligomerisation levels in plasma of people with type 2 diabetes

    Rehn, F., et al.

    Sci Rep 14:19556 (2024).

  • Aβ oligomers peak in early stages of Alzheimer’s disease preceding tau pathology

    Blömeke, L. et al.

    Alzheimers Dement (Amst), 16(2), e12589 (2024).

  • Disrupted-in-schizophrenia 1 protein aggregates in cerebrospinal fluid are elevated in patients with first-episode psychosis

    Pils, M. et al.

    Psychiatry Clin Neurosci 77, 665–671 (2023).

  • Patients with isolated REM-sleep behavior disorder have elevated levels of alpha-synuclein aggregates in stool

    Schaffrath, A. et al.

    NPJ Parkinsons Dis 9, 14 (2023).

  • Development and Implementation of an Internal Quality Control Sample to Standardize Oligomer-Based Diagnostics of Alzheimer’s Disease

    Pils, M. et al.

    Diagnostics (Basel) 13(10), 1702 (2023).

  • Oral treatment with the all-d-peptide RD2 enhances cognition in aged beagle dogs – A model of sporadic Alzheimer’s disease

    Kutzsche, J. et al.

    Heliyon 9, e18443 (2023).

  • Tau protein aggregation associated with SARS-CoV-2 main protease

    Eberle, R. J. et al.

    PLoS One 18, e0288138 (2023).

  • Abeta oligomer concentration in mouse and human brain and its drug-induced reduction ex vivo

    Kass, B. et al.

    Cell Rep Med 3, 100630 (2022).

  • Quantitative detection of alpha-Synuclein and Tau oligomers and other aggregates by digital single particle counting

    Blomeke, L. et al.

    NPJ Parkinsons Dis 8, 68 (2022).

  • Abeta Oligomer Elimination Restores Cognition in Transgenic Alzheimer’s Mice with Full-blown Pathology

    Schemmert, S. et al.

    Mol Neurobiol 56, 2211-2223 (2019).

  • Advancements of the sFIDA method for oligomer-based diagnostics of neurodegenerative diseases

    Kulawik, A., Heise, H., Zafiu, C., Willbold, D. & Bannach, O.

    FEBS Lett 592, 516-534 (2018).

  • Analysis of anticoagulants for blood-based quantitation of amyloid beta oligomers in the sFIDA assay

    Kravchenko, K. et al.

    Biol Chem 398, 465-475 (2017).

  • sFIDA automation yields sub-femtomolar limit of detection for Abeta aggregates in body fluids

    Herrmann, Y. et al.

    Clin Biochem 50, 244-247 (2017).

  • Nanoparticle standards for immuno-based quantitation of alpha-synuclein oligomers in diagnostics of Parkinson’s disease and other synucleinopathies

    Herrmann, Y. et al.

    Chim Acta 466, 152-159 (2017).

  • Application of an Amyloid Beta Oligomer Standard in the sFIDA Assay

    Kuhbach, K. et al.,

    Front Neurosci 10, 8 (2016).

  • The amyloid-beta oligomer count in cerebrospinal fluid is a biomarker for Alzheimer’s disease.

    Wang-Dietrich, L. et al.,

    J Alzheimers Dis 34, 985-994 (2013).

  • Biofunctionalized Silica Nanoparticles: Standards in Amyloid-beta Oligomer-Based Diagnosis of Alzheimer’s Disease

    Hulsemann, M. et al.,

    J Alzheimers Dis 54, 79-88 (2016).

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