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Home Biotechnologies New fluorescent marker for pathological amyloid protein aggregates

New fluorescent marker for pathological amyloid protein aggregates


Aggregation of soluble proteins into highly ordered beta-sheet fibrillar structures, termed amyloids, is a key factor in etiology of a number of the so-called conformational diseases, including Alzheimer's, Parkinson's, Huntingtons diseases, type II diabetes, rheumatoid arthritis, spongiform encephalophaties, etc.

The main techniques currently employed to identify amyloid protein aggregates involve electron microscopy and fluorescence spectroscopy. Classical fluorescent marker for amyloid is benzothiazole dye Thioflavin T (TT). However, ThT assay is not devoid of shortcomings associated, particularly, with
i) dependence of ThT spectral characteristics on fibril morphology, pH, ionic strength;
ii) ThT ability to affect fibrillization kinetics and stability of fibrillar intermediates;
iii) sensitivity of ThT fluorescence to the presence of exogenous compounds, for instance, polyphenols.

By testing a wide variety of fluorophores of various classes it was found that aminoderivative of benzanthrone, 3-morpholino-7H-benzo[de]anthracene-7-one (ABM) displays photophysical characteristics allowing to considerably increase sensitivity and specificity of amyloid detection, to improve interpretation of the assay results, to reduce material and time costs. Due to its properties, such as
i) large Stokes shift;
ii) high extinction coefficient;
iii) very weak fluorescence in an aqueous phase;
iv) high specificity of complexation with amyloids, ABM represents a very promising amyloid marker.

ABM is localized in the cavities, channels or grooves, abundant in the structure of amyloid fibrils. This gives rise to substantial increase of the probe fluorescence intensity upon its association with amyloids and permits differentiation between the fluorescence signals from ABM bound to fibrillar structures and native protein.

Innovative Aspect and Main Advantages

The use of new fluorescent amyloid marker ABM will permit:

  • to increase sensitivity of detection of pathological protein aggregates due to higher ABM affinity for amyloid fibrils and weaker binding to the native protein compared to classical amyloid marker Thioflavin T;
  • to improve accuracy of experimental measurements by lowering the contribution of light scattering to fluorescence signal;
  • to reduce the amyloid assay cost due to the use of very small probe concentrations.

Areas of Application

Medical diagnostics, medical imaging, amyloid studies

Fig. 1 Fluorescence microscopy imaging of fibrillar aggregates formed in albumin-lipid systems

Stage of Development

Prototype available for testing

Contact Details

Contact person: Galyna Gorbenko
V.N. Karazin Kharkov National University, Department of Biological and Medical Physics
Address: Svobody sq.4, Kharkov, 61077
Tel/Fax: (380-57) 343-82-44
Mob.: 8(050) 859-62-31
E-mail: This e-mail address is being protected from spambots. You need JavaScript enabled to view it

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