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Your search keyword '"Tretyakova, Iryna"' showing total 14 results
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14 results on '"Tretyakova, Iryna"'

1. Synthesis and spectral properties of mixed-ligand Zr and Hf phthalocyanine complexes with out-of-plane coordinated alkylamino-β-ketoenolate chromophores and decanoate

Author

Chernii, Viktor, primary, Tretyakova, Iryna, additional, Fedosova, Natalia, additional, Dovbii, Yan, additional, Chernii, Svitlana, additional, Losytskyy, Mykhaylo, additional, Gorski, Aleksander, additional, Starukhin, Alexandr, additional, Pekhnyo, Vasyl, additional, and Kovalska, Vladyslava, additional

Published
2024
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13. Study of tetraphenylporphyrins as modifiers of insulin amyloid aggregation.

Author

Chernii, Svitlana, Losytskyy, Mykhaylo, Kelm, Anna, Gorski, Alexandr, Tretyakova, Iryna, Yarmoluk, Sergiy, Chernii, Victor, and Kovalska, Vladyslava

Subjects
INSULIN, AMYLOID, AMINO group
Abstract

Amyloid fibrils are rigid β‐pleated protein aggregates that are connected with series of harmful diseases and at the same time are promising as base for novel nanomaterials. Thus, design of compounds able to inhibit or redirect those aggregates formation is important both for the biomedical aims and for nanotechnology applications. Here, we studied the effect of tetraphenylporphyrins (metal free, their Cu and Pd complexes, and those functionalized by carboxy and amino groups on periphery) on insulin amyloid self‐assembling. The strongest impact on insulin aggregation was demonstrated by a metal‐free porphyrin bearing four carboxy groups. This compound strongly suppresses insulin aggregation (about 88% reduction in amyloid‐sensitive probe emission) inducing formation of fibrils with the length close to this of free insulin (1.7 ± 0.6 μm as compared with 1.4 ± 0.4 μm, respectively) with an essentially reduced tendency to lateral aggregation. Contrarily, the presence of tetraphenylporphyrin containing four amino groups only slightly affects fibrils' morphology and makes weaker impact on insulin aggregation yield (about 44% reduction). This is explained by the ability of aromatic carboxy groups of 5,10,15,20‐(tetra‐4‐carboxyphenyl)porphyrin to interact with complementary protein‐binding groups and thus stabilize the supramolecular complex. For 5,10,15,20‐(tetra‐4‐aminophenyl)porphyrin, full protonation takes place in acidic medium of protein aggregation reaction; this results in the high positive charge of TPPN4 (equal or close to +6) and hence higher contribution of coulombic repulsion to interaction of TPPN4 with insulin. One more possible mechanism of the lower inhibition effect of TPPN4 as compared with TPPC4 could be the more restricted possibility of the former as compared with the latter to form H bonds with insulin groups. It was also shown that metal‐free, Pd‐containing, and Cu‐containing tetraphenylporphyrins without peripheral substituents make almost the same impact on the protein self‐assembling. We suppose this to be due to coordination saturation of these metal atoms. [ABSTRACT FROM AUTHOR]

Published
2020
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14. β-ketoenole dyes: synthesis and study as fluorescent sensors for protein amyloid aggregates

Author

Chernii, Svitlana, Vladyslava Kovalska, Losytskyy, Mykhaylo, Dovbii, Yan, Tretyakova, Iryna, Czerwieniec, Rafal, Chernii, Victor, Yarmoluk, Sergiy, and Volkov, Sergiy

Subjects
β-ketoenole dyes, fluorescent sensing, probes, amyloid fibrils, insulin, lysozime, proteins, 3. Good health
Abstract

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 105 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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