2020
DOI: 10.1039/d0dt00209g
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Homo- and heteroleptic trimethoxy terpyridine–Cu(ii) complexes: synthesis, characterization, DNA/BSA binding, DNA cleavage and cytotoxicity studies

Abstract: In the current study, four novel mononuclear Cu(ii) complexes with terpyridine (L) and different co-ligands (phen, bipy, and imd) were synthesized and characterized in detail, where L is 4′-(3,4,5-trimethoxyphenyl)-2,2′:6′,2′′-terpyridine.

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Cited by 33 publications
(23 citation statements)
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“…The decrease in fluorescence intensity of EtBr and ctDNA at 617 nm (Figure c) was examined by estimating the binding constant value using the Stern–Volmer equation where I 0 and I are emission intensities measured at the emission wavelength of 617 nm for [EtBr + ctDNA] and [EtBr + ctDNA + C-dots], respectively.…”
Section: Resultsmentioning
confidence: 99%
“…The decrease in fluorescence intensity of EtBr and ctDNA at 617 nm (Figure c) was examined by estimating the binding constant value using the Stern–Volmer equation where I 0 and I are emission intensities measured at the emission wavelength of 617 nm for [EtBr + ctDNA] and [EtBr + ctDNA + C-dots], respectively.…”
Section: Resultsmentioning
confidence: 99%
“… [214] 48-Cu AGE,pET-28b, e OxC * Cytotoxicity activity. [66] 49-Ru 4 pCMUT, AGE, PC *Photocytotoxicity activity: MTT assay. Cellular ROS generation.…”
Section: Amss In Pharma Studiesmentioning
confidence: 99%
“…Accordingly, these actively ongoing techniques are categorized as follow: i) Preparation of multinuclear complexes wherein the metal cores cooperate to provides an efficient active binding site for biomolecules [56] , [57] , [58] , [59] , [60] , [61] , [62] , [63] , [64] , [65] . ii) Variation of the first coordination sphere towards synthesis of homoleptic and hetroleptic complexes [66] , [67] , [68] , [69] , [70] , [71] . iii) Modification of the second coordination sphere via addition of the functional groups or by using the supramolecular hosts such as cyclodextrins (CDs) [56] , [57] , [72] , [73] , [74] , [75] , [76] , [77] , [78] , [79] , [80] , [81] , [82] , [83] .…”
Section: Introductionmentioning
confidence: 99%
“…The BSA protein is sub-divided into three parts for the drugs to bind, out of which one is located at the sub-domain IIA which contains the tryptophan and tyrosine residues while the other two is located at IIIA sub-domain which contains only the tyrosine residue. [86] Further, the complex and BSA when interact, it results in the changes of these protein residues and the spectra (Figure 8) shows significant quenching of fluorescence which is indicative of strong binding occurring along with either conformational changes, decreasing hydrophobicity or increasing the polarity of the BSA molecule. [73,85,87,88] Since a clear involvement of tryptophan residues can be seen in the spectra at Δλ = 60 nm, one can conclude that sub-domain IIA will probably be the binding site of the protein.…”
Section: Syntheses and Characterization Of Ruthenium Pincer Complexes...mentioning
confidence: 99%