Corrigendum to “Half sandwiched RutheniumII complexes: En Route towards the targeted delivery by Human Serum Albumin (HSA)” [J. Organomet. Chem. 937 (2021) 121732]

Hairat, Suboot; Zaki, Mehvash

doi:10.1016/j.jorganchem.2021.121834

Cited by 3 publications

(4 citation statements)

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“…Circular dichroism (CD) spectra were recorded to assess whether the complex‘s interaction with HSA induces changes in the protein‘s secondary structure. HSA′s structure mainly consists of α‐helices, and its CD spectra exhibit two negative bands in the UV region, specifically at 222 and 208 nm [61,62] . Therefore, conformational changes of the protein caused by the interaction with the complex can be analyzed by changes in HSA CD spectra in the absence and presence of 1 [62] .…”

Section: Resultsmentioning

confidence: 99%

“…HSA′s structure mainly consists of α‐helices, and its CD spectra exhibit two negative bands in the UV region, specifically at 222 and 208 nm [61,62] . Therefore, conformational changes of the protein caused by the interaction with the complex can be analyzed by changes in HSA CD spectra in the absence and presence of 1 [62] . No significant modifications on the HSA CD spectra were observed upon addition of 1 (Figure SI12), indicating that the interaction between complex and HSA by hydrogen bonds occurs with no (or very small) changes on protein's secondary structure.…”

Section: Resultsmentioning

confidence: 99%

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Water‐Soluble μ‐oxo triruthenium Compound of Biological Interest: H‐Bonds Network and Interaction with HSA

Pinheiro,

Fernandes,

Chaves

et al. 2024

Eur J Inorg Chem

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The water‐soluble compound [Ru3O(CH3COO)6(4‐ampy)3]Cl (1, 4‐ampy = 4‐aminopyridine) was evaluated in terms of its biologically relevant properties. Compound 1 participates in a hydrogen bonding network which includes the NH2 substituents of the ancillary ligands, methanol molecules, the Cl‐ counter‐ion, and a non‐conventional hydrogen bond with the neighboring 4‐ampy molecules' π‐cloud, as determined by X‐ray measurements. One protonation equilibrium was observed at pH values below 2.3. Additionally, the compound exhibited a partition coefficient value of ‐0.86 (± 0.07), indicating that it is highly hydrophilic. At 370C and pH = 7.4 (phosphate buffer), compound 1 shows moderate (Ksv = 2.4 104 M‐1) and spontaneous (ΔG = ‐26.4 kJ mol‐1) binding to human serum albumin (HSA) through ground‐state association, which involves formation of hydrogen bonds (ΔH = ‐35.7 kJ mol‐1 and,ΔS = ‐29.8 J mol‐1 K‐1). Molecular docking calculations support the formation of hydrogen bonds between 1 and HSA, and suggest subdomain IIA (site I), which contains the Trp‐214 residue, as the primary interactive pocket, in agreement with the experimental static fluorescence quenching mechanism. Furthermore, a preliminary assay reveals that 1 has low cytotoxicity towards human glioblastoma U87‐MG cells.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Water‐Soluble μ‐oxo triruthenium Compound of Biological Interest: H‐Bonds Network and Interaction with HSA

Pinheiro,

Fernandes,

Chaves

et al. 2024

Eur J Inorg Chem

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“…The strength of this interaction will determine how the drug will be transported and delivered to a certain target. [24,45,47,49,50] To address an eventual interaction and to assign the quenching mechanism beyond any doubts, [38,51] we measured the HSA lifetimes in the presence of different amounts of 1 or 2, at different temperatures (Figures SI 7 and 8). The data are listed in Table 2.…”

Section: Chemistryselectmentioning

confidence: 99%

Interactions with HSA, anticancer and antiallergic activity of binuclear μ‐oxo bridged ruthenium acetate compounds

et al. 2023

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The μ‐oxo bridged ruthenium acetate 1 [Ru2O(CH3COO)2(5‐CH3‐1,10‐phen)2(py)2](PF6)2 (5‐CH3‐1,10‐phen=5‐methyl‐1,10‐phenanthroline; py=pyridine) is presented. Its electronic and infrared spectra, as well as its cyclic voltammograms are all consistent with the proposed structure. Regarding biological properties, we collected data for 1 and its analog [Ru2O(CH3COO)2(1,10‐phen)2(py)2](PF6)2 (2) to infer the role of phenantroline methylation. The HSA fluorescence is quenched by 1 and the presence of variable concentrations of it did not affect the τ1/2 values for the HSA excited state lifetime (mean τ1/2 values=3.56, 3.46, and 3.32 ns at 298, 304, and 310 K respectively). Circular dichroism showed that the HSA α‐helix content decreased only 5 % upon interaction with 1, which formed a ground‐state adduct with HSA, not changing the protein structure to a significant extent. Interaction between 1 and DNA was weak; Benesi‐Hildebrand constants were in the order of 102 M−1. We probed the allergenic potential/antiallergic activity of 1, observing that 200 μM inhibited mast cell degranulation by about 80 %, while cell viability remained unaltered throughout the measurement (2 h). Therefore, 1 has antiallergic potential and is not an allergen. Regarding its anticancer activity, at all the employed concentrations, 1 was more cytotoxic than 2 against B16F10 murine melanoma cancer cells. At 25 μM, 1 reduced cell viability to less than 14 %, while 2 reduced cell viability to only 78 %.

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“…75 Measuring the relative extent of this quenching has provided significant insight into the affinity of HSA for various small molecules, including Ru(II)-arene complexes. 76 To determine the binding affinity of each complex for HSA, increasing amounts of each complex were mixed with a standard solution of HSA followed by incubation for 1 hour at 37 °C, after which fluorescence measurements were taken.…”

Section: Binding To Human Serum Albuminmentioning

confidence: 99%

A Ru(ii)-arene-ferrocene complex with promising antibacterial activity

et al. 2022

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Corrigendum to “Half sandwiched RutheniumII complexes: En Route towards the targeted delivery by Human Serum Albumin (HSA)” [J. Organomet. Chem. 937 (2021) 121732]

Cited by 3 publications

References 0 publications

Water‐Soluble μ‐oxo triruthenium Compound of Biological Interest: H‐Bonds Network and Interaction with HSA

Water‐Soluble μ‐oxo triruthenium Compound of Biological Interest: H‐Bonds Network and Interaction with HSA

Interactions with HSA, anticancer and antiallergic activity of binuclear μ‐oxo bridged ruthenium acetate compounds

A Ru(ii)-arene-ferrocene complex with promising antibacterial activity

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