Studying the interaction between trinuclear ruthenium complexes and human serum albumin by means of fluorescence quenching

Cacita, Natacha; Nikolaou, Sofia

doi:10.1016/j.jlumin.2015.08.066

Cited by 57 publications

(47 citation statements)

References 41 publications

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“…[20] In addition to the most commonly investigated use in the solar cells, emerge applications of ruthenium based dyes in other scientific fields, for example, in biomedicine. [1][2][3][4][5][6][7] Ruthenium (II) complexes were shown to bind to DNA defects [7] as well as to be a quantitative DNA detectors. [3] Recently, a number of studies have suggested them as a potential photodynamic agents in the cancer therapy, [4][5][6] live-cell imaging, [21,22] ATP (adenosine-5'-triphosphate) detection, [1] interaction with HSA (human serum albumin), [2] and theranostic applications.…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopy of zinc oxide nanoplatelets modified with ruthenium (II) complexes

Ristić‐Djurović

Fernández‐Izquierdo

Hadžić

et al. 2019

J Raman Spectroscopy

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We analyzed and compared the unmodified and three modified zinc oxide nanoplatelet materials. The three components used in zinc oxide modification were the 4,4apos;‐bipyridine and two ruthenium (II) complexes, namely, the trans‐[Ru (bpy)(bpyCOO)Cl2]2– and cis‐[Ru (bpy)(bpyCOO)Cl2]2–. The obtained results revealed that after modification, ZnO nanoplatelets became smaller and embedded in the materials used for the modification. When ZnO was modified with either of the two ruthenium (II) complexes, the interaction between them led to a higher activity of ZnO. The metal‐to‐ligand charge transfer that was also detected in the two cases of ZnO nanoplatelets modified with the ruthenium (II) complexes caused significant alteration of the Raman spectrum and consequent changes of the optical properties. Various forms of ruthenium (II) complexes were used in several published studies related to dye‐sensitized solar cells and biomedicine. The biomedical applications include, for example, the ATP (adenosine‐5apos;‐triphosphate) detection, interaction with human serum albumin, DNA analysis, and cancer detection and treatment. The properties of the ZnO nanoplatelets modified with the two ruthenium (II) complexes presented here indicate that it may be worth exploring if the studied materials are applicable in the dye sensitized solar cells and biomedicine. Possible advantage of our results is that they were obtained at room temperature.

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Section: Introductionmentioning

confidence: 99%

Raman spectroscopy of zinc oxide nanoplatelets modified with ruthenium (II) complexes

Ristić‐Djurović

Fernández‐Izquierdo

Hadžić

et al. 2019

J Raman Spectroscopy

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“…The strongest ability of quenching is exhibited by Pd [138] and Ru [23,36,52] in binding with albumins and by Cu [44][45][46][47]49,141] in binding with DNA. Minimum quenching constants are observed in binding of albumins with and Pd [150] : pK = 2, and DNA with Ru [151] : pK = 1-2.…”

Section: Discussionmentioning

confidence: 99%

“…The major attention in the case of metal complexes binding with proteins is paid to the therapeutic properties, and only in some cases the binding parameters were studied which, if necessary, were improved by changing temperature [8,23,[33][34][35][36][37][38][39] or selecting organic and inorganic coligands (mostly 1,10-phenantholine and bipyridyl) which bind with a complexing metal together with a drug molecule. [8,24,36,37,[39][40][41][42][43][44][45][46][47][48][49][50][51][52][53][54] The complexes under study are mainly biligand complexes containing a drug ligand and coligand. The Figure 3 shows the distribution of the studing from the viewpoint of metals studied.…”

Section: Metal Complexesmentioning

confidence: 99%

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Supramolecular interaction of transition metal complexes with albumins and DNA: Spectroscopic methods of estimation of binding parameters

Galkina

Проскурнин

2018

Applied Organom Chemis

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Binding parameters of metal complexes with albumins and DNA since the middle of 1990s are considered and summarized. The most widespread spectroscopic methods of estimation of binding parameters are discusseddirect fluorescent methods, indirect fluorescent methods (by fluorescence quenching parameters), and ways of estimation of binding constants by other optical spectroscopic methods. The methods and approaches to calculations used for the determination of binding constants are discussed. The data on the already found binding constants and kinetic parameters is systematized.KEYWORDS albumins, DNA, metal complexes, proteins, supramolecular interaction Funding information: Russian Foundation for Basic Research, Grant/Award Number: 16-03-01089_a 16-53-50027_YaF_a Abbreviations and designations used: F 0 , fluorescence intensity in the absence of a quencher; F, fluorescence intensity in the presence of a acid); NTSC, a new thiosemicarbazone; o-cbiaH, 5-(2-carboxybenzyloxy)isophthalic acid; o-van-gln, a Schiff base derived from o-vanillin and glutamine; o-van-L-met, Schiff base derived from o-vanillin and L-methionine; oxo, 5-

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“…It is known that linear Stern-Volmer plots indicate one type of quenching mechanism as predominant, either static or dynamic [30]. Moreover, in Table 1, the values of Kq at different temperatures were much higher than the limiting diffusion rate constant of biomolecules (k d ≈ 2.0 × 10 10 M −1 ·s −1 ) [31][32][33][34], which revealed static quenching via forming a complex. For a complex formation process, the affinity constant K a of the binding between FDQL and HSA was analyzed by modified Stern-Volmer Equation (2) [35][36][37]:…”

Section: Fluorescence Quenching Mechanismmentioning

confidence: 92%

Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

Zhu

et al. 2016

Molecules

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Abstract:In the present study, 3-(fluorobenzylideneamino)-6-chloro-1-(3,3-dimethylbutanoyl)-phenyl-2,3-dihydroquinazolin-4(1H)-one (FDQL) derivatives have been designed and synthesized to study the interaction between fluorine substituted dihydroquinazoline derivatives with human serum albumin (HSA) using fluorescence, circular dichroism and Fourier transform infrared spectroscopy. The results indicated that the FDQL could bind to HSA, induce conformation and the secondary structure changes of HSA, and quench the intrinsic fluorescence of HSA through a static quenching mechanism. The thermodynamic parameters, ∆H, ∆S, and ∆G, calculated at different temperatures, revealed that the binding was through spontaneous and hydrophobic forces and thus played major roles in the association. Based on the number of binding sites, it was considered that one molecule of FDQL could bind to a single site of HSA. Site marker competition experiments indicated that the reactive site of HSA to FDQL mainly located in site II (subdomain IIIA). The substitution by fluorine in the benzene ring could increase the interactions between FDQL and HSA to some extent in the proper temperature range through hydrophobic effect, and the substitution at meta-position enhanced the affinity greater than that at para-and ortho-positions.

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Studying the interaction between trinuclear ruthenium complexes and human serum albumin by means of fluorescence quenching

Cited by 57 publications

References 41 publications

Raman spectroscopy of zinc oxide nanoplatelets modified with ruthenium (II) complexes

Raman spectroscopy of zinc oxide nanoplatelets modified with ruthenium (II) complexes

Supramolecular interaction of transition metal complexes with albumins and DNA: Spectroscopic methods of estimation of binding parameters

Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

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