Journal ArticleDOI
Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity.
Vitali I. Stsiapura,A. A. Maskevich,V. A. Kuzmitsky,Vladimir N. Uversky,Irina M. Kuznetsova,Konstantin K. Turoverov +5 more
TLDR
The photophysical model successfully explains the fluorescent properties of ThT in solvents with different viscosities and supports the idea that the reason for the characteristic increase in the ThT fluorescence intensity accompanying its incorporation into the amyloid fibrils is determined by the rigidity of the dye environment.Abstract:
The effect of solvent viscosity on thioflavin T (ThT) fluorescent properties is analyzed to understand the molecular mechanisms of the characteristic increase in ThT fluorescence intensity accompanying its incorporation into the amyloid-like fibrils. To this end, the dependencies of the ThT quantum yield and fluorescence lifetime on temperature and glycerol content in the water−glycerol mixtures are studied. It has been found that fluorescent properties of ThT are typical for the specific class of fluorophores known as molecular rotors. It has been established that the low ThT fluorescence intensity in the solvents with low viscosity is caused by the nonradiative deactivation of the excited state associated with the torsional motion of the ThT benzthiazole and aminobenzene rings relative to each other, which results in the transition of ThT molecule to nonfluorescent twisted internal charge transfer (TICT) state. The rate of this process is determined by the solvent viscosity, whereas the emission does oc...read more
Citations
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Journal ArticleDOI
Solvent viscosity induces twisted intramolecular charge transfer state lifetime tunable of Thioflavin-T.
TL;DR: This work provides a comprehensive understanding of fluorescence molecular rotor (FMR) deactivation process in different viscosity solvents and is helpful to design new FMR.
Journal ArticleDOI
Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates
TL;DR: A large number of novel protein supramolecular structures are being designed and tested as highly performing biomaterials, with a clear advantage provided by the intrinsic biocompatibility and...
Journal ArticleDOI
Fluorescence detection of cationic amyloid fibrils in human semen
David Easterhoff,John DiMaio,Wathsala Liyanage,Chi-Wen Lo,Woori Bae,Todd M. Doran,Alan V. Smrcka,Bradley L. Nilsson,Stephen Dewhurst +8 more
TL;DR: This work performed high-throughput screening to identify molecules that bind SEVI, and identified a small molecule (8E2), that fluoresced brightly in the presence of SEVI and other cationic fibrils.
Journal ArticleDOI
Effect of pH on the structure and function of pyruvate dehydrogenase kinase 3: Combined spectroscopic and MD simulation studies.
Saleha Anwar,Rajiv K. Kar,Md. Anzarul Haque,Rashmi Dahiya,Preeti Gupta,Asimul Islam,Faizan Ahmad,Md. Imtaiyaz Hassan +7 more
TL;DR: The significance of structural dependence of pH for wide implications in protein-protein interaction, biological function and drug design procedures is highlighted, and a well defined correlation was observed between experimental and computational studies.
Journal ArticleDOI
Oxidation of thiamine on reaction with nitrogen dioxide generated by ferric myoglobin and hemoglobin in the presence of nitrite and hydrogen peroxide.
TL;DR: After addition of tyrosine or phenol to aqueous solutions containing oxoferryl forms of the hemoproteins, thiamine, and nitrite, the yield of thiochrome greatly increased, whereas theield of ODTch decreased, as well as antioxidant properties of the hydrophobicThiamine metabolitesThiochrome and O DTch are discussed.
References
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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.
TL;DR: Thioflavine T associates rapidly with aggregated fibrils of the synthetic β/A4‐derived peptides β( 1–28) and β(1–40), giving rise to a new excitation maximum at 450 nm and enhanced emission at 482 nm, as opposed to the 385 nm and 445 nm of the free dye.
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