Multi experimental and computational studies for DNA and HSA interaction of new nano-scale ultrasound-assisted synthesized Pd(II) complex as a potent anticancer drug

Dehkhodaei, Monireh; Sahihi, Mehdi; Rudbari, Hadi Amiri; Ariaeefar, Mahnaz; Gharaghani, Sajjad; Azadbakht, Reza; Taheri, Salman; Kajani, Abolghasem Abbasi

doi:10.1016/j.molliq.2018.05.077

Cited by 14 publications

(9 citation statements)

References 69 publications

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“…Depending on the structure of the interacting molecule, CD spectroscopy may reveal important alterations in the secondary HSA structure by variations in the absorption at 208 nm, as recently reported for a polynuclear ruthenium carboxylate [56] . On the other hand, literature also brings examples where the interacting molecules do not significantly alter the protein secondary structure as probed by CD spectra, with very little variation on α‐helix content [57–62] . This is because, although HSA fluorescence quenching is an actual signal of interaction, it might happen from a purely collisional mechanism or from non‐specific interactions on the surface of the protein.…”

Section: Resultsmentioning

confidence: 91%

“…[56] On the other hand, literature also brings examples where the interacting molecules do not significantly alter the protein secondary structure as probed by CD spectra, with very little variation on α-helix content. [57][58][59][60][61][62] This is because, although HSA fluorescence quenching is an actual signal of interaction, it might happen from a purely collisional mechanism or from non-specific ) 2 is able to efficiently quench HSA fluorescence, it causes very slight changes in its secondary structure. There is a very small decreasing trend for the α-helix content (from 64.9 % to 63.5 % from absence of complex to four-fold excess) and no significant changes in the β-sheet and random coil percentages.…”

Section: Resultsmentioning

confidence: 99%

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Interactions of a Ruthenium‐Ketoprofen Compound with Human Serum Albumin and DNA: Insights from Spectrophotometric Titrations and Molecular Docking Calculations

Sarmento

Pinheiro

Abrahão³

et al. 2022

ChemistrySelect

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The compound [Ru 2 O(keto) 2 (py) 6 ](PF 6 ) 2 , keto = ketoprofen and py = pyridine, interacts with calf thymus-DNA with K b = 1.08 × 10 4 M À 1 . It efficiently quenches HSA fluorescence in different temperatures, with Ksv values in the 10 4 -10 5 M À 1 range, both by dynamic and static mechanisms. The data provided by the double logarithmic and van't Hoff approximations indicated a moderate (K b � 10 4 M À 1 ) and spontaneous (ΔG < 0) interaction, being enthalpically driven (ΔH = À 27.1 kJ mol À 1 and ΔS = À 5.3 J mol À 1 K À 1 ). Molecular docking calculations confirmed that the binuclear compound interacts with HSA more strongly than with DNA. The occurrence of a high contribution from electrostatic forces was observed, fully consistent with the bicationic nature of [Ru 2 O(keto) 2 (py) 6 ](PF 6 ) 2 . The molecular docking results also revealed that the interaction occurs in an external subdomain, explaining the lack of significant conformational changes in the protein, as probed by circular dichroism spectra.

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Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Interactions of a Ruthenium‐Ketoprofen Compound with Human Serum Albumin and DNA: Insights from Spectrophotometric Titrations and Molecular Docking Calculations

Sarmento

Pinheiro

Abrahão³

et al. 2022

ChemistrySelect

View full text Add to dashboard Cite

show abstract

“…Changes in the intensity at 208 nm points to conformational changes in the protein upon interaction with small molecules. However, reports have shown that interacting molecules with the ability to quench the HSA fluorescence may not significantly modify the protein secondary structure, with only discrete variations in the α‐helix content taking place [54–58] . This observation usually holds when the investigated molecule exclusively engages in non‐specific interactions on the protein surface.…”

Section: Resultsmentioning

confidence: 99%

“…( ChemistrySelect molecules with the ability to quench the HSA fluorescence may not significantly modify the protein secondary structure, with only discrete variations in the α-helix content taking place. [54][55][56][57][58] This observation usually holds when the investigated molecule exclusively engages in non-specific interactions on the protein surface. This is the case of the only previous reported case of a [Ru 2 O] compound interacting with HSA, [24] where variations in the α-helix content were even smaller.…”

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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“…8−10 The Pd(II) complexes have previously been found to exhibit potent anticancer properties against a wide range of cancer cell lines, particularly those resistant to cisplatin. 11,12 The ultimate target of the metal-based drugs is the DNA owing to the covalent intra-strand binding mode of cisplatin with DNA, not only the cancer cell proliferation is inhibited, the normal cells are also being damaged, which is responsible for toxicity and side effects. This work is mainly focused on designing and developing anticancer lead molecules based on palladium and regulating the mode of bonding of the metal complex with DNA through a non-covalent interaction, either intercalation or groove binding.…”

Section: ■ Introductionmentioning

confidence: 99%

Anticancer Behavior of Pyrrolidine-Based Palladium(II) Complexes and Biophysical Approach on Their DNA, BSA Binding Activity, Molecular Docking, and DFT Study

et al. 2023

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A series of pyrrolidine-based Pd(II) complexes, [Pd(AEP)Cl 2 ] (C-1), [Pd(AEP)(OH 2 ) 2 ] 2+ (C-2), [Pd(AEP)(Lcys)] + (C-3), [Pd(AEP)(N-ac-L-cys)] (C-4), [Pd(AEP)(GSH)] (C-5), and [Pd(AEP)(DL-meth)] 2+ (C-6) (where, AEP = 1-(2aminoethyl)pyrrolidine, L-cys = L-cysteine, N-ac-L-cys = N-acetyl-L-cysteine, GSH = glutathione, and DL-meth = DL-methionine), as anticancer drug candidates have been synthesized and characterized. The DNA binding property of the complexes was executed by gel electrophoresis and spectrophotometric and viscometric methods, and their interaction with BSA was also investigated by various spectroscopic methodologies. The binding activity of the Pd(II) complexes with DNA and BSA were assessed to evaluate their binding mode and binding constants. Molecular docking was performed to correlate with the experimental results on the interaction of the complexes with DNA and BSA. The changes in the microenvironmental and structural properties of BSA are monitored by a synchronous and 3D fluorescence study. The structural properties were evaluated by DFT and TD-DFT studies. The anticarcinogenic activity of the Pd(II) complexes was assessed by PASS prediction software to corroborate with the experimental results of the anticancer activity of the complexes. The ROS generation in cancer cell lines has been investigated, and the cell death mechanism through apoptosis was confirmed by measuring the protein expression. All these complexes have excellent anticancer activity compared to ancillary ligands. The cancer cell line (HCT116) shows almost similar or better cell inhibition activity when treated with the Pd(II) complexes compared to cisplatin, whereas the adverse effect is minimum on a normal cell (NKE). Both the Pd(II) and Pt(II) complexes carrying the same ligands reveal almost similar antiproliferative activity.

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Multi experimental and computational studies for DNA and HSA interaction of new nano-scale ultrasound-assisted synthesized Pd(II) complex as a potent anticancer drug

Cited by 14 publications

References 69 publications

Interactions of a Ruthenium‐Ketoprofen Compound with Human Serum Albumin and DNA: Insights from Spectrophotometric Titrations and Molecular Docking Calculations

Interactions of a Ruthenium‐Ketoprofen Compound with Human Serum Albumin and DNA: Insights from Spectrophotometric Titrations and Molecular Docking Calculations

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

Anticancer Behavior of Pyrrolidine-Based Palladium(II) Complexes and Biophysical Approach on Their DNA, BSA Binding Activity, Molecular Docking, and DFT Study

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