Half sandwiched RutheniumII complexes: En Route towards the targeted delivery by Human Serum Albumin (HSA)

Hairat, Suboot; Zaki, Mehvash

doi:10.1016/j.jorganchem.2021.121732

Cited by 15 publications

(5 citation statements)

References 180 publications

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“…For example, arene has been widely used as a ligand, as it can stabilize the oxidation state of metal complexes. Hence, a series of hydrophilic and hydrophobic arene Ru(II/III) complexes have been designed and synthesized with great potential for the development of metal-based chemotherapeutic drugs [ 18 , 19 ]. There are few studies focused on Ru(IV) complexes that search for efficient anticancer candidates.…”

Section: Introductionmentioning

confidence: 99%

Ruthenium Complexes as Promising Candidates against Lung Cancer

Sun

Shi

et al. 2021

Molecules

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Lung cancer is one of the most common malignancies with the highest mortality rate and the second-highest incidence rate after breast cancer, posing a serious threat to human health. The accidental discovery of the antitumor properties of cisplatin in the early 1960s aroused a growing interest in metal-based compounds for cancer treatment. However, the clinical application of cisplatin is limited by serious side effects and drug resistance. Therefore, other transition metal complexes have been developed for the treatment of different malignant cancers. Among them, Ru(II/III)-based complexes have emerged as promising anticancer drug candidates due to their potential anticancer properties and selective cytotoxic activity. In this review, we summarized the latest developments of Ru(II/III) complexes against lung cancer, focusing mainly on the mechanisms of their biological activities, including induction of apoptosis, necroptosis, autophagy, cell cycle arrest, inhibition of cell proliferation, and invasion and metastasis of lung cancer cells.

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Section: Introductionmentioning

confidence: 99%

Ruthenium Complexes as Promising Candidates against Lung Cancer

Sun

Shi

et al. 2021

Molecules

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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: Resultsmentioning

confidence: 99%

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

et al. 2022

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“…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: Interaction With Human Serum Albuminmentioning

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 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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Half sandwiched RutheniumII complexes: En Route towards the targeted delivery by Human Serum Albumin (HSA)

Cited by 15 publications

References 180 publications

Ruthenium Complexes as Promising Candidates against Lung Cancer

Ruthenium Complexes as Promising Candidates against Lung Cancer

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

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

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