Trans-2-[4-(dimethylamino)styryl]-3-ethyl-1,3-benzothiazolium perchlorate - New fluorescent dye for testing of amyloid fibrils and study of their structure

2018 ◽  
Vol 157 ◽  
pp. 385-395 ◽  
Author(s):  
Anna I. Sulatskaya ◽  
Maksim I. Sulatsky ◽  
Olga I. Povarova ◽  
Natalia P. Rodina ◽  
Irina M. Kuznetsova ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Fluorescent Dye

Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T

1989 ◽  
Vol 177 (2) ◽  
pp. 244-249 ◽  
Author(s):  
Hironobu Naiki ◽  
Keiichi Higuchi ◽  
Masanori Hosokawa ◽  
Toshio Takeda
Keyword(s):  
Amyloid Fibrils ◽  
Fluorescent Dye ◽  
Fluorometric Determination ◽  
Thioflavine T

scholarly journals The Fluorescent Dye 1,6-Diphenyl-1,3,5-Hexatriene Binds to Amyloid Fibrils Formed by Human Amylin and Provides a New Probe of Amylin Amyloid Kinetics

2021 ◽  
Author(s):  
Ming-Hao Li ◽  
Lakshan Manathunga ◽  
Erwin London ◽  
Daniel Raleigh
Keyword(s):  
Time Course ◽  
Amyloid Fibrils ◽  
Fold Increase ◽  
Fluorescent Dye ◽  
Thioflavin T ◽  
Lag Phase ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Human Amylin ◽  
Mutant Forms

The fluorescent dye 1,6-diphenyl-1,3,5-hexatriene (DPH) is widely used as a probe of membrane order. We show that DPH also interacts with amyloid fibrils formed by human amylin (also known as islet amyloid polypeptide) in solution and this results in a 100-fold increase in DPH fluorescence for a sample of microM human amylin and 0.25 microM DPH. No increase in DPH fluorescence is observed with the non-amyloidogenic rat amylin or with freshly dissolved, non-fibrillar human amylin. The time course of amyloid formation by amylin was followed by monitoring the fluorescence of added DPH as a function of time and was similar to that monitored by the standard fluorescent probe thioflavin-T. The inclusion of DPH in the buffer did not perturb the time course of amyloid formation under the conditions examined and the time course was independent of the range of DPH concentrations tested (0.25 to 5 microM). Maximum final fluorescence intensity is observed at substoichiometric ratios of DPH to amylin. No significant increase in fluorescence was observed during the lag phase of amyloid formation, and the implications for the structure of amylin pre-fibril oligomers are discussed. Human amylin contains three aromatic residues. A triple aromatic to leucine mutant forms amyloid and DPH binds to the resulting fibrils, indicating that interactions with aromatic side chains are not required for DPH amylin amyloid interactions. DPH may be especially useful for studies on mutant amylins and other polypeptides in which changes in charged residues might complicate interpretation of thioflavin-T fluorescence.

scholarly journals Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T

2018 ◽  
Vol 19 (9) ◽  
pp. 2762 ◽  
Author(s):  
Anna Sulatskaya ◽  
Natalia Rodina ◽  
Dmitry Polyakov ◽  
Maksim Sulatsky ◽  
Tatyana Artamonova ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amyloid Fibrils ◽  
Biological Fluids ◽  
Fluorescent Dye ◽  
Full Length ◽  
Thioflavin T ◽  
Protein Amino Acid ◽  
Terminal Amino ◽  
Beta 2 ◽  
Beta 2 Microglobulin

The persistence of high concentrations of beta-2-microglobulin (β2M) in the blood of patients with acute renal failure leads to the development of the dialysis-related amyloidosis. This disease manifests in the deposition of amyloid fibrils formed from the various forms of β2M in the tissues and biological fluids of patients. In this paper, the amyloid fibrils formed from the full-length β2M (β2m) and its variants that lack the 6 and 10 N-terminal amino acids of the protein polypeptide chain (ΔN6β2m and ΔN10β2m, respectively) were probed by using the fluorescent dye thioflavin T (ThT). For this aim, the tested solutions were prepared via the equilibrium microdialysis approach. Spectroscopic analysis of the obtained samples allowed us to detect one binding mode (type) of ThT interaction with all the studied variants of β2M amyloid fibrils with affinity ~104 M−1. This interaction can be explained by the dye molecules incorporation into the grooves that were formed by the amino acids side chains of amyloid protofibrils along the long axis of the fibrils. The decrease in the affinity and stoichiometry of the dye interaction with β2M fibrils, as well as in the fluorescence quantum yield and lifetime of the bound dye upon the shortening of the protein amino acid sequence were shown. The observed differences in the ThT-β2M fibrils binding parameters and characteristics of the bound dye allowed to prove not only the difference of the ΔN10β2m fibrils from other β2M fibrils (that can be detected visually, for example, by transmission electron microscopy (TEM), but also the differences between β2m and ΔN6β2m fibrils (that can not be unequivocally confirmed by other approaches). These results prove an essential role of N-terminal amino acids of the protein in the formation of the β2M amyloid fibrils. Information about amyloidogenic protein sequences can be claimed in the development of ways to inhibit β2M fibrillogenesis for the treatment of dialysis-related amyloidosis.

Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red

2011 ◽  
Vol 7 (4) ◽  
pp. 1232 ◽  
Author(s):  
Rajesh Mishra ◽  
Daniel Sjölander ◽  
Per Hammarström
Keyword(s):  
Amyloid Fibrils ◽  
Nile Red ◽  
Spectroscopic Characterization ◽  
Fluorescent Dye

Liquid crystalline ordering of paired helical filaments in neurofibrillary tangles of Alzheimer's disease

1986 ◽  
Vol 44 ◽  
pp. 348-349
Author(s):  
D.F. Clapin ◽  
V.J.A. Montpetit
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neurofibrillary Tangles ◽  
Liquid Crystalline ◽  
Amyloid Fibrils ◽  
Geometric Analysis ◽  
Paired Helical Filaments ◽  
Microscopic Level ◽  
Light Microscopic Level ◽  
Regular Spacing

Alzheimer's disease is characterized by the accumulation of abnormal filamentous proteins. The most important of these are amyloid fibrils and paired helical filaments (PHF). PHF are located intraneuronally forming bundles called neurofibrillary tangles. The designation of these structures as "tangles" is appropriate at the light microscopic level. However, localized domains within individual tangles appear to demonstrate a regular spacing which may indicate a liquid crystalline phase. The purpose of this paper is to present a statistical geometric analysis of PHF packing.

3-Dimensional immunolabeling and in situ hybridization detection using fluorescence photooxidation and intermediate-voltage Electron Microscopy

1994 ◽  
Vol 52 ◽  
pp. 164-165
Author(s):  
Thomas J. Deerinck ◽  
Maryann E. Martone ◽  
Varda Lev-Ram ◽  
David P. L. Green ◽  
Roger Y. Tsien ◽  
...  
Keyword(s):  
Laser Scanning ◽  
Reactive Oxygen ◽  
Confocal Laser Scanning Microscope ◽  
Fluorescent Dye ◽  
Confocal Laser ◽  
3 Dimensional ◽  
Voltage Electron ◽  
Dimensional Distribution ◽  
Electron Microscopes ◽  
New Generation

The confocal laser scanning microscope has become a powerful tool in the study of the 3-dimensional distribution of proteins and specific nucleic acid sequences in cells and tissues. This is also proving to be true for a new generation of high contrast intermediate voltage electron microscopes (IVEM). Until recently, the number of labeling techniques that could be employed to allow examination of the same sample with both confocal and IVEM was rather limited. One method that can be used to take full advantage of these two technologies is fluorescence photooxidation. Specimens are labeled by a fluorescent dye and viewed with confocal microscopy followed by fluorescence photooxidation of diaminobenzidine (DAB). In this technique, a fluorescent dye is used to photooxidize DAB into an osmiophilic reaction product that can be subsequently visualized with the electron microscope. The precise reaction mechanism by which the photooxidation occurs is not known but evidence suggests that the radiationless transfer of energy from the excited-state dye molecule undergoing the phenomenon of intersystem crossing leads to the formation of reactive oxygen species such as singlet oxygen. It is this reactive oxygen that is likely crucial in the photooxidation of DAB.

Use of Indocyanine Green Fluorescent Dye Video Angiography in Orthopaedic Trauma: A Pilot Study

2013 ◽  
Vol 22 (04) ◽  
pp. 310-315 ◽  
Author(s):  
CPT Andrew Cleveland ◽  
Amr Abdelgawad ◽  
Jonathan Cook ◽  
Miguel Pirela-Cruz
Keyword(s):  
Pilot Study ◽  
Indocyanine Green ◽  
Fluorescent Dye ◽  
Orthopaedic Trauma ◽  
Green Fluorescent
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