The adsorption of an anticancer hydrazone by protein: an unusual static quenching mechanism

Tian, Fang; Li, Jia-Han; Jiang, Feng-Lei; Han, Xiaojiao; Chen, Xiang; Ge, Yushu; Li, Lili; Liu, Yi

doi:10.1039/c1ra00521a

Cited by 75 publications

(30 citation statements)

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“…As showed in Scheme 1, synthesis route to CPBH is the one-pot synthesis developed in our previous works [68,69]. Briefly, hydrazine hydrate (1.0 mmol) was added to a solution of methyl-4-chlorobenzoate (1.0 mmol) in 10mL ethanol.…”

Section: Preparationmentioning

confidence: 99%

“…The bioactivities of hydrazones especially acylhydrazones have been studied for a long time, and we have found that hydrazones possessed excellent ability to form complex with metal ions [68,69], since there are many nitrogen and oxygen atoms in the molecules of hydrazones working as donor atoms. If we add some chromophores into the molecule of acylhydrazones, it could meet the requirement discussed above pretty well.…”

Section: Introductionmentioning

confidence: 99%

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Fabrication of an acylhydrazone based fluorescence probe for Al3+

Liu

Tian

Fan

et al. 2017

Sensors and Actuators B: Chemical

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Section: Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Fabrication of an acylhydrazone based fluorescence probe for Al3+

Liu

Tian

Fan

et al. 2017

Sensors and Actuators B: Chemical

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“…Therefore, the process of quenching the fluorescence of HSA interacting with EFHB is mediated primarily by a static mechanism. [4,5,[44][45][46] A Table 3. [47] The K a values for EFHB are 10 4 L mol -1 , suggesting very strong binding to HSA at the range of temperature studied.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…The K a values obtained in the present study are consistent with previous literature reports to systems HSA-Hydrazones. [4][5][6][7] 0,0 5,0x10 4 1,0x10 5 1,5x10 5 2,0x10 5 2,5x10 5 3,0x10 5 3,5x10 5 The number of bound complex HSA-EFHB (n) were determined by plotting the double log graph of the fluorescence data using. [47] Plotting log((F 0 -F)/F) Vs log [Q] according to equation 4, it was obtained a straight line whose slope denotes the number of interaction sites that may have in the formation of the HSA-EFBH complex ( Figure 9).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…Equation 2 describes a straight line when graphing the F 0 /F ratio as a function of [Q] at different temperatures;this implies that the mechanism of quenching the intrinsic fluorescence of a biomolecule occurs through a homogeneous process, a static or dynamic mechanism [20,41]. and F are the fluorescence intensities of the biomolecule in the absence and presence quencher respectively, K SV is the Stern-Volmer quenching constant, [Q] is the molar concentration of quencher, k q is the quenching rate constant of biological macromolecule, τ 0 is the average excited state lifetime of HSA without quencher, that is,5.78 x 10 -9 s [20]. By plotting the relation of the fluorescence F 0 /F against the [Q] a…”

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Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods

Morales-Toyo

Glidewell

Bruno-Colmenares

et al. 2019

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Please cite this article as: M. Morales-Toyo, C. Glidewell, J. Bruno-Colmenares, et al., Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods, Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, https://doi. AbstractA novel hydrazone, (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate (EFHB), has been synthesized and characterized by FT-IR, NMR and Mass spectroscopy, and Xray diffraction; compound crystallized as translucent light yellow thin plates. EFHB was studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Addition of this hydrazone to HSA ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T2 produced significant fluorescence quenching and splitting of emission spectra of HSA through static quenching mechanism with binding constants of about 10 4 M -1 at 292. 15, 298.15, 304.15 and 310.15 K. According to the synchronous fluorescence, tryptophan and tyrosine residues of the protein are most perturbed by the binding process.Thermodynamic parameters ΔG, ΔH, and ΔS were got and the main sort of acting force between EFHB and HSA was studied. Results of molecular docking have shown that EFHB binds to subdomain IIA of HSA mainly by hydrophobic interaction, energy binding are in good agreement with those obtained by fluorescence study (ΔG the = -7.32 ± 0.09 kcal mol -1 and ΔG exp = -6.76 ± 0.03 kcal mol -1 ).

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Tridentate Schiff base and 4,4′‐bipyridine coordinated di/polynuclear Cu (II) complexes: Synthesis, crystal structure, DNA/protein binding and catecholase activity

Bhunia

Bertolasi

Manna

2020

Applied Organom Chemis

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4,4′‐bipyridine bridged two Cu (II) complexes, [Cu2L12(4,4′‐bipy)(H2O)2](ClO4)2 (1) and [Cu2L22(4,4′‐bipy)]n·(2H2O)n (2) (where, HL1 = 2‐[(3‐methylamino‐propylimino)‐methyl]‐phenol, H2L2 = 3‐[(2‐hydroxy‐3‐methoxy‐benzylidene)‐amino]‐propionic acid, and 4,4′‐bipy = 4,4′‐bipyridine) have been synthesized and characterized by single crystal structure determination, mass spectrometry, FT‐IR, electronic absorption, and emission spectroscopy. Complex 1 is dinuclear cationic compound and counter balanced by perchlorate anion, whereas complex 2 possesses 1D poly‐nuclear structure. Both the complexes crystallize in monoclinic system with P21/c space group and the copper centers possess square pyramidal geometry. H‐bonding, C‐H···π, π···π interactions results the formation of two dimentional supramolecular structure for both the complexes. Interactions of complexes with bovine serum albumins (BSA) and human serum albumins (HSA) have been studied by using electronic absorption and emission spectroscopic technique. The calculated values of binding constants (Kb) are (9.22 ± 0.26) × 105 L mol−1 (1‐BSA), (7.19 ± 0.16) × 105 L mol−1 (1‐HSA), (5.05 ± 0.20) × 105 L mol−1 (2‐BSA) and (3.56 ± 0.25) × 105 L mol−1 (2‐HSA). The mechanism of serum albumins‐complex interactions have been investigated by fluorescence lifetime measurement. Fluorescence spectroscopic studies indicate that both the complexes interact with calf thymas‐DNA. Catecholase activity of the complexes has been studied in methanol using 3,5‐di‐tert‐butylcatechol (3,5‐DTBC) as substrate and the result show that both the complexes are active for catalytic oxidation of 3,5‐DTBC to 3,5‐di‐tert‐butylquinone (3,5‐DTBQ) in presence of molecular oxygen. Calculated values of turnover numbers are 71.81 ± 1.04 h−1 and 69.45 ± 0.74 h−1 for 1 and 2, respectively.

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The adsorption of an anticancer hydrazone by protein: an unusual static quenching mechanism

Cited by 75 publications

References 50 publications

Fabrication of an acylhydrazone based fluorescence probe for Al3+

Fabrication of an acylhydrazone based fluorescence probe for Al3+

Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods

Tridentate Schiff base and 4,4′‐bipyridine coordinated di/polynuclear Cu (II) complexes: Synthesis, crystal structure, DNA/protein binding and catecholase activity

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