Tri- and Pentamethine Cyanine Dyes for Fluorescent Detection of α-Synuclein Oligomeric Aggregates

Kovalska, Vladyslava; Losytskyy, Mykhaylo Yu.; Tolmachev, O.I.; Slominskii, Yu. L.; Segers-Nolten, Gezina M.J.; Subramaniam, Vinod; Yarmoluk, S. M.

doi:10.1007/s10895-012-1081-x

Cited by 33 publications

(21 citation statements)

References 29 publications

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“…As for Aβ and tau, fluorescence methods have successfully been employed for the sensitive and specific detection of intermolecular interactions. Structure‐based non‐covalent fluorescent probes have been developed to specifically detect the presence of oligomers, or pre‐fibrillar species during aggregation . Alternatively, fluorophores have been conjugated to specific sites of αS using maleimide chemistry on cysteine residues inserted by site‐specific mutagenesis on the αS polypeptide chain .…”

Section: Alpha‐synuclein and Parkinson's Diseasementioning

confidence: 99%

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

et al. 2018

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The link between protein aggregation and neurodegenerative disease is well established. However, given the heterogeneity of species formed during the aggregation process, it is difficult to delineate details of the molecular events involved in generating pathological aggregates from those producing soluble monomers. As aberrant aggregates are possible pharmacological targets for the treatment of neurodegenerative diseases, the need to observe and characterise soluble oligomers has pushed traditional biophysical techniques to their limits, leading to the development of a plethora of new tools capable of detecting soluble oligomers with high precision and specificity. In this review, we discuss a range of modern biophysical techniques that have been developed to study protein aggregation, and give an overview of how they have been used to understand, in detail, the aberrant aggregation of amyloidogenic proteins associated with the two most common neurodegenerative disorders, Alzheimer's disease and Parkinson's disease.

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Section: Alpha‐synuclein and Parkinson's Diseasementioning

confidence: 99%

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

et al. 2018

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“…[11, [34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][50]), a considerable number of other fluorogenic stains have been shown to illuminate amyloids (e.g. [11,[51][52][53][54][55][56][57][58][59][60][61][62][63][64][65][66][67]). In particular, Nilsson and colleagues have developed a number of novel fluorescent amyloidogenic markers.…”

Section: Introductionmentioning

confidence: 99%

Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker^™stains

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Hendricks

et al. 2017

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In recent work, we discovered that the presence of highly substoichiometric amounts (10 -8 molar ratio) of lipopolysaccharide (LPS) from Gram-negative bacteria caused fibrinogen clotting to lead to the formation of an amyloid form of fibrin. We here show that the broadly equivalent lipoteichoic acids (LTAs) from two species of Gram-positive bacteria have similarly (if not more) potent effects. Using thioflavin T fluorescence to detect amyloid as before, the addition of low concentrations of free ferric ion is found to have similar effects. Luminescent conjugated oligothiophene dyes (LCOs), marketed under the trade name Amytracker TM , also stain classical amyloid structures. We here show that they too give very large fluorescence enhancements when clotting is initiated in the presence of the four amyloidogens (LPS, ferric ions and two LTA types). The staining patterns differ significantly as a function of both the amyloidogens and the dyes used to assess them, indicating clearly that the nature of the clots formed is different. This is also the case when clotting is measured viscometrically using thermoelastography. Overall, the data provide further evidence for an important role of bacterial cell wall products in the various coagulopathies that are observable in chronic, inflammatory diseases. The assays may have potential in both diagnostics and therapeutics.

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“…The histological dyes Congo Red and Chrysamine G are used for the staining and study of amyloid formations on tissues [5][6][7]. Recently we discovered and developed mono and polymethine cyanines dyes as efficient fluorescent probes for the detection of protein β-pleated aggregates [8,9]. Cyanines with high sensitivity to the amyloid fibrils and wide detection range (1.5-120 µg/ml for trimethine cyanine 7519 [10]) surpassing that of Thioflavine T were proposed.…”

Section: Introductionmentioning

confidence: 99%

β-ketoenole dyes: Synthesis and study as fluorescent sensors for protein amyloid aggregates

et al. 2016

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The series of the new β-ketoenole dyes ((2E,5Z,7E,9E)-6-hydroxy-2-(alkylamino)-10-phenyldeca-2,5,7,9-tetraen-4-ones) with variation of alkylamino tail groups was synthesized and studied as potential probes for the sensing of protein aggregates amyloid fibrils. The dyes are low fluorescent when free but able to increase their emission intensity in dozens of times in the presence of fibrillar insulin. The fluorescent response of the dye on fibrillar insulin strongly depends on the nature of the alkylamino tail group. For compounds with propylamino (dye 13) and 2-hydroxyethylamino (dye 14) fragments the fluorescence intensity in the presence of fibrillar insulin exceeds that for the native one in 22 and 66 times correspondingly. However dyes demonstrate from low or moderate exceed of the fluorescence intensity in the presence of aggregated lysozyme compared to native one (up to 8.7 times for the dye 53 bearing methyl ester tail group), due to their pronounced sensitivity to native lysozyme. The dyes in complexes with insulin have rather height quantum yield up to 0.15, the large Stokes shifts values (about 100 nm and more), their binding constant values are about 10 5 M -1 . The dye 14 allows fluorescent detection of the insulin amyloid fibrils in the concentration range 1-50 μg/ml. This causes an interest in the future study of the β-ketoenole as prospective fluorescent amyloid-sensitive molecules.

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Tri- and Pentamethine Cyanine Dyes for Fluorescent Detection of α-Synuclein Oligomeric Aggregates

Cited by 33 publications

References 29 publications

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker^™stains

β-ketoenole dyes: Synthesis and study as fluorescent sensors for protein amyloid aggregates

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Tri- and Pentamethine Cyanine Dyes for Fluorescent Detection of α-Synuclein Oligomeric Aggregates

Cited by 33 publications

References 29 publications

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

Shedding light on aberrant interactions – a review of modern tools for studying protein aggregates

Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker™stains

β-ketoenole dyes: Synthesis and study as fluorescent sensors for protein amyloid aggregates

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Product

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Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker^™stains