Integrated experimental/computational approaches to characterize the systems formed by vanadium with proteins and enzymes

Sciortino, Giuseppe; Maréchal, Jean‐Didier; Garribba, Eugenio

doi:10.1039/d0qi01507e

Cited by 29 publications

(23 citation statements)

References 186 publications

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“…On the other hand, recent developments in theoretical techniques were achieved to predict the covalent and noncovalent binding of a vanadium moiety to a protein; such an approach, combined with spectrometric and spectroscopic methods, has been also applied to the VCs–protein systems with encouraging results. 29 …”

Section: Discussionmentioning

confidence: 99%

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A

et al. 2021

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The structure, stability, and enzymatic activity of the adduct formed upon the reaction of the V–picolinato (pic) complex [V IV O(pic) 2 (H 2 O)], with an octahedral geometry and the water ligand in cis to the V=O group, with the bovine pancreatic ribonuclease (RNase A) were studied. While electrospray ionization-mass spectrometry, circular dichroism, and ultraviolet–visible absorption spectroscopy substantiate the interaction between the metal moiety and RNase A, electron paramagnetic resonance (EPR) allows us to determine that a carboxylate group, stemming from Asp or Glu residues, and imidazole nitrogen from His residues are involved in the V binding at acidic and physiological pH, respectively. Crystallographic data demonstrate that the V IV O(pic) 2 moiety coordinates the side chain of Glu111 of RNase A, by substituting the equatorial water molecule at acidic pH. Computational methods confirm that Glu111 is the most affine residue and interacts favorably with the OC -6-23-Δ enantiomer establishing an extended network of hydrogen bonds and van der Waals stabilizations. By increasing the pH around neutrality, with the deprotonation of histidine side chains, the binding of the V complex to His105 and His119 could occur, with that to His105 which should be preferred when compared to that to the catalytically important His119. The binding of the V compound affects the enzymatic activity of RNase A, but it does not alter its overall structure and stability.

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Section: Discussionmentioning

confidence: 99%

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A

et al. 2021

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“…Representative binding isotherms for the investigated systems are shown in Figure 3, whereas conditional parameters of the interactions are summarized in Table 1. (1) Literature data [17].…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

“…It is also worth highlighting that albumins are one of the main objects of study in the field of bioinorganic-and metallo-drug design [15][16][17]. However, in the frame of biological studies, cell culture media used in cytotoxicity assays of new compounds usually contain relatively high amount of BSA (ca.…”

Section: Introductionmentioning

confidence: 99%

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

et al. 2021

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The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)4]−) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)4]− for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)4]− ions (logK(ITC)1 = 7.09 ± 0.10; ΔG(ITC)1 = −9.67 ± 0.14 kcal mol−1; ΔH(ITC)1 = −3.14 ± 0.12 kcal mol−1; TΔS(ITC)1 = −6.53 kcal mol−1), whereas the second site is localized in the subdomain III A and binds five ions (logK(ITC)2 = 5.39 ± 0.06; ΔG(ITC)2 = −7.35 ± 0.09 kcal mol−1; ΔH(ITC)2 = 4.00 ± 0.14 kcal mol−1; TΔS(ITC)2 = 11.3 kcal mol−1). The formation of the {[B(Ph)4]−}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.

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“…The results obtained in the interactions between decavanadate and diprotonated decavanadate with the pre-miR-21 RNA, even though the interactions remain the same, yet the binding energies are slightly improved in the diprotonated decavanadate by 1 kcal/mol. As for the interaction with RNA and DNA molecules, it indicates an excellent possibility to induce brakes due to ROS generation as reduction of vanadium(V) to vanadium (IV) will take place in the cytosol, as ascorbic acid and reduced glutathione will react with vanadium species ( Levina and Lay 2017 ; Costa-Pessoa and Correia 2021 ; Sciortino et al, 2021 ; Sanna et al, 2021 ; Sanna et al, 2021 ; Aureliano et al, 2021 ). Our recent findings of decavanadate interacting with bases such as cytosine, DMAP, and 2-aminopyridine, point to a high affinity of decavanadate to form stable hydrogen bonds with protonated nitrogenous bases or with water molecules serving as a bridge.…”

Section: Discussionmentioning

confidence: 99%

Tris(2-Pyridylmethylamine)V(O)2 Complexes as Counter Ions of Diprotonated Decavanadate Anion: Potential Antineoplastic Activity

et al. 2022

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The synthesis and theoretical-experimental characterization of a novel diprotanated decavanadate is presented here due to our search for novel anticancer metallodrugs. Tris(2-pyridylmethyl)amine (TPMA), which is also known to have anticancer activity in osteosarcoma cell lines, was introduced as a possible cationic species that could act as a counterpart for the decavanadate anion. However, the isolated compound contains the previously reported vanadium (V) dioxido-tpma moieties, and the decavanadate anion appears to be diprotonated. The structural characterization of the compound was performed by infrared spectroscopy and single-crystal X-ray diffraction. In addition, DFT calculations were used to analyze the reactive sites involved in the donor-acceptor interactions from the molecular electrostatic potential maps. The level of theory mPW1PW91/6–31G(d)-LANL2DZ and ECP = LANL2DZ for the V atom was used. These insights about the compounds’ main interactions were supported by analyzing the noncovalent interactions utilizing the AIM and Hirshfeld surfaces approach. Molecular docking studies with small RNA fragments were used to assess the hypothesis that decavanadate’s anticancer activity could be attributed to its interaction with lncRNA molecules. Thus, a combination of three potentially beneficial components could be evaluated in various cancer cell lines.

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Integrated experimental/computational approaches to characterize the systems formed by vanadium with proteins and enzymes

Abstract: Decoding the interactions of transition metal complexes with proteins is still an open challenge in many fields like biology and medicinal chemistry or in the design of de novo enzymes,...

Cited by 29 publications

References 186 publications

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Tris(2-Pyridylmethylamine)V(O)2 Complexes as Counter Ions of Diprotonated Decavanadate Anion: Potential Antineoplastic Activity

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Integrated experimental/computational approaches to characterize the systems formed by vanadium with proteins and enzymes

Abstract: Decoding the interactions of transition metal complexes with proteins is still an open challenge in many fields like biology and medicinal chemistry or in the design of de novo enzymes,...

Cited by 29 publications

References 186 publications

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the VIVO–Picolinato Complex with RNase A

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the VIVO–Picolinato Complex with RNase A

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Tris(2-Pyridylmethylamine)V(O)2 Complexes as Counter Ions of Diprotonated Decavanadate Anion: Potential Antineoplastic Activity

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Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A

Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V^IVO–Picolinato Complex with RNase A