Interaction of apo-transferrin with anticancer ruthenium complexes NAMI-A and its reduced form

Mazuryk, Olga; Kurpiewska, Katarzyna; Lewiński, K.; Stochel, Grażyna; Brindell, Małgorzata

doi:10.1016/j.jinorgbio.2012.07.017

Cited by 48 publications

(61 citation statements)

References 33 publications

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“…All measured binding constants are approximately in the order of 10 5 M −1 ; these are higher constants compared with ruthenium complexes which are in the order of 10 3 M −1 -10 4 M −1 [21,40,41].…”

Section: Association Between the Complex And The Transferrin Effect mentioning

confidence: 82%

“…This type of deviation occurs when quencher molecules interact with tryptophan and tyrosine residues causing the fluorescence quenching; then they change their position within the fluorophore microenvironment making room for the other molecules of the quencher. Further, it has been recently demonstrated in similar systems that the contribution of dynamic quenching seems to be less than the static quenching [21]. …”

Section: Quenching Experimentsmentioning

confidence: 98%

“…This implies that the transferrin-drug system needs to preserve a proper affinity for the transferrin receptor so as to facilitate its interaction. It has been shown that transferrin promotes uptake of Ru(III) complexes into tumor cells [21]. Therefore, these properties of Tf have motivated us to investigate its interaction with polypyridyl Cr(III) complexes in order to evaluate whether this protein could act as a potential carrier of Cr(III) complexes to tumor cells.…”

Section: Introductionmentioning

confidence: 99%

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Binding of [Cr(phen)3]3+ to transferrin at extracellular and endosomal pHs: Potential application in photodynamic therapy

García¹,

Toneatto²,

Silvero³

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Section: Association Between the Complex And The Transferrin Effect mentioning

confidence: 82%

Section: Quenching Experimentsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Binding of [Cr(phen)3]3+ to transferrin at extracellular and endosomal pHs: Potential application in photodynamic therapy

García¹,

Toneatto²,

Silvero³

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

View full text Add to dashboard Cite

“…The mode of action and the intracellular targets of Ru(III) complexes are not exactly known. There are many investigations suggesting that the intravenously injected drugs can be transported mainly by the serum albumin and/or transferrin in the blood plasma [14][15][16][17][18]. Reduction of Ru (III) compounds in the cytosol leads to the kinetically more labile and more reactive Ru (II) compounds.…”

Section: [Tetrachlorido(1h-imidazole)(dimethylsulfoxide-κs)ruthenate(mentioning

confidence: 99%

Solution equilibrium studies of anticancer ruthenium(II)-η6-p-cymene complexes of pyridinecarboxylic acids

et al. 2014

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Stoichiometry and stability of antitumor ruthenium(II)-η 6 -p-cymene complexes of picolinic acid and its 6-methyl and 6-carboxylic acid derivatives were determined by pHpotentiometry, 1 H NMR spectroscopy and UV/Vis spectrophotometry in aqueous solution in the presence or absence of coordinating chloride ions. The picolinates form exclusively monoligand complexes in which they can coordinate via the bidentate (O,N) mode and a chloride or a water molecule is found at the third binding site of the ruthenium(II)-η 6 -p-cymene moiety depending on the conditions. [Ru(η 6 -p-cymene)(L)(H 2 O/Cl)] species are predominant at physiological pH in all studied cases. Hydrolysis of the aqua complex or the chlorido/hydroxido co-ligand exchange results in the formation of the mixed-hydroxido species [Ru(η 6 -p-cymene)(L)(OH)] in the basic pH range. There is no indication for the decomposition of the mono-ligand complexes during 24 h in the ruthenium(II)-η 6 -pcymene−picolinic acid system between pH 3 and 11; however, a slight dissociation with a low reaction rate was found in the other two systems leading to the appearance of the dinuclear trihydroxido-bridged species [Ru 2 (η 6 -p-cymene) 2 (OH) 3 ] + and free ligands at pH > 10. The replacement of the chlorido by an aqua ligand in [Ru(η 6 -p-cymene)(L)Cl] was also monitored and equilibrium constants for the exchange process were determined.

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“…Rapid binding to Tf was reported by Speiewak et al because the equilibrium could be reached within 5 min in fluorescence Tyr quenching experiments [234]. Binding constants of logK = 4.11 [234,244] and 4.01 [234] were determined for apoTf and holoTf, respectively, and coordination at other sites was suggested in addition to the Fe(III) binding sites [234]. Similar to NKP-1339, HSA is also the major binder for NAMI-A in blood serum.…”

Section: Anticancer Ru(iii) Complexes In Serummentioning

confidence: 69%

Development of the application of speciation in chemistry

Kiss

Enyedy

Jakusch

2017

Coordination Chemistry Reviews

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Interaction of apo-transferrin with anticancer ruthenium complexes NAMI-A and its reduced form

Cited by 48 publications

References 33 publications

Binding of [Cr(phen)3]3+ to transferrin at extracellular and endosomal pHs: Potential application in photodynamic therapy

Binding of [Cr(phen)3]3+ to transferrin at extracellular and endosomal pHs: Potential application in photodynamic therapy

Solution equilibrium studies of anticancer ruthenium(II)-η6-p-cymene complexes of pyridinecarboxylic acids

Development of the application of speciation in chemistry

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