Structural and Photodynamic Studies on Nitrosylruthenium-Complexed Serum Albumin as a Delivery System for Controlled Nitric Oxide Release

Xie, Leilei; Bai, Hehe; Song, Luna; Liu, Chenyang; Gong, Wenjun; Wang, Wenming; Zhao, Xuan; Takemoto, Chie; Wang, Hongfei

doi:10.1021/acs.inorgchem.1c00762

Cited by 11 publications

(6 citation statements)

References 96 publications

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“…Tunability of the structure of MOFs, reviewed by Seabra and Duran, also allows for controlled release of NO for specific biological applications . Finally, many ls-{RuNO} 6 and ls-{MnNO} 6 complexes have shown utility as light-triggered NO delivery platforms for photodynamic therapy. ,,,− …”

Section: Nitric Oxide In Mammalian Signaling and Immune Defensementioning

confidence: 99%

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of physiological and pathological events in biology. Metal coordination chemistry, especially with iron, is at the heart of many biological transformations involving NO. A series of heme proteins, nitric oxide synthases (NOS), soluble guanylate cyclase (sGC), and nitrophorins, are responsible for the biosynthesis, sensing, and transport of NO. Alternatively, NO can be generated from nitrite by heme- and copper-containing nitrite reductases (NIRs). The NO-bearing small molecules such as nitrosothiols and dinitrosyl iron complexes (DNICs) can serve as an alternative vehicle for NO storage and transport. Once NO is formed, the rich reaction chemistry of NO leads to a wide variety of biological activities including reduction of NO by heme or non-heme iron-containing NO reductases and protein post-translational modifications by DNICs. Much of our understanding of the reactivity of metal sites in biology with NO and the mechanisms of these transformations has come from the elucidation of the geometric and electronic structures and chemical reactivity of synthetic model systems, in synergy with biochemical and biophysical studies on the relevant proteins themselves. This review focuses on recent advancements from studies on proteins and model complexes that not only have improved our understanding of the biological roles of NO but also have provided foundations for biomedical research and for bio-inspired catalyst design in energy science.

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Section: Nitric Oxide In Mammalian Signaling and Immune Defensementioning

confidence: 99%

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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“…The HSA molecule is a single-chain protein which contains 585 amino acid residues in a heart-like shape, and the three domains in HSA provide binding sites for a wide variety of endogenous ligands ( Ghuman et al, 2005 ; Xie et al, 2021 ). To examine the number of the Fe complex bound to HSA in solution, the native and Fe complex–treated HSA were analyzed by MALDI-TOF MS.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopy, Structure, Biomacromolecular Interactions, and Antiproliferation Activity of a Fe(II) Complex With DPA-Bpy as Pentadentate Ligand

et al. 2022

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An Fe(II) complex with DPA-Bpy (DPA-Bpy = N,N-bis(2-pyridinylmethyl)-2,20-bipyridine-6 -methanamine) as the ligand was synthesized and characterized to mimic bleomycin. The binding constants (Kb) of the complex with calf thymus DNA and human serum albumin (HSA) were quantitatively evaluated using fluorescence spectroscopy, with Kb as 5.53×105 and 2.40×104 M−1, respectively; the number of the average binding site (n) is close to 1. The thermodynamic analyses suggested that the electrostatic interactions exist between the complex and DNA, and the hydrogen bonding and Van der Waals force exist for the complex and HSA. The Fe complex exhibits cleavage ability toward pBR322 DNA, and the crystal structure of the HSA Fe complex adduct at 2.4 Å resolution clearly shows that His288 serves as the axial ligand of the Fe center complexed with a pentadentate DPA-Bpy ligand. Furthermore, the cytotoxicity of the complex was evaluated against HeLa cells. Both the Fe complex and HSA Fe complex adduct show obvious effect on cell proliferation with an IC50 of 1.18 and 0.82 μM, respectively; they induced cell apoptosis and arrested cell cycles at S phase. This study provides insight into the plausible mechanism underlying their metabolism and pharmacological activity.

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“…16, PDB ID: ). 63,208,209 It should be noted that two other structures of HSA adducts with ruthenium complexes were also reported, namely HSA-[RuCl 5 (indazole)] 2− , 208 and HSA-[RuCl 4 (indazole) 2 ] − . 209…”

Section: Ruthenium Nitrosyl Complexes As Potential Anticancer Drugsmentioning

confidence: 88%

“…16, PDB ID: 7DL4). 63,208,209 It should be noted that two other structures of HSA adducts with ruthenium complexes were also reported, namely HSA-[RuCl 5 (indazole)] 2− , 208 and HSA-[RuCl 4 (indazole) 2 ] − . 209 The investigation of the photoinduced inactivation of DNA repair enzymes (DNA glycosylases) in vitro by [RuNO(L) 2 (NO 2 ) 2 OH], where L = 3-methylpyridine, 210 revealed that the activity of DNA glycosylases decreased by more than 90% after irradiation.…”

Section: Dalton Transactions Perspectivementioning

confidence: 92%

“…Human serum albumin (HSA) as a delivery vehicle for controlled nitric oxide release was investigated on nitrosyl ruthenium complexes [RuCl 3 (L 1 )(NO)] − , where HL 1 = 8-hydroxyquinoline and its derivatives 62,63,208,209 and [RuCl(L 1 )(L 2 )(NO)] + , where HL 1 = 8-hydroxyquinoline, L 2 = 2,2′-bipyridine derivative. 204 The binding constants of the ruthenium complexes with HSA (as well as DNA) were determined by fluorescence spectroscopy.…”

Section: Dalton Transactions Perspectivementioning

confidence: 99%

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Ruthenium-nitrosyl complexes as NO-releasing molecules, potential anticancer drugs, and photoswitches based on linkage isomerism

et al. 2022

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Structural and Photodynamic Studies on Nitrosylruthenium-Complexed Serum Albumin as a Delivery System for Controlled Nitric Oxide Release

Cited by 11 publications

References 96 publications

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

Spectroscopy, Structure, Biomacromolecular Interactions, and Antiproliferation Activity of a Fe(II) Complex With DPA-Bpy as Pentadentate Ligand

Ruthenium-nitrosyl complexes as NO-releasing molecules, potential anticancer drugs, and photoswitches based on linkage isomerism

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