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The reaction of the cytotoxic compound dirhodium tetraacetate with a B-DNA double helical dodecamer was studied by X-ray crystallography and mass spectrometry. The structure of the dirhodium/DNA adduct reveals a dimetallic center binding to an adenine axial coordination. Complementary information has been gained through ESI MS measurements. Comparison between the present data and those previously obtained for cisplatin indicates that the two metallodrugs react with this DNA dodecamer in a significantly different fashion.
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http://dx.doi.org/10.1039/d3dt00320e | DOI Listing |
Int J Mol Sci
July 2025
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.
Paddlewheel dirhodium complexes are cytotoxic compounds that are also used as catalysts and in the formation of Rh-based artificial metalloenzymes. Low-temperature structures of adducts formed by the model protein hen egg white lysozyme (HEWL) with dirhodium tetraacetate ([Rh(μ-OCCH)]) when crystals of the protein were treated with the metal compound at 20 °C demonstrated that [Rh(μ-OCCH)] in part breaks down upon reaction with HEWL; dimeric Rh-Rh units bind the side chains of Asp18 and the C-terminal carboxylate, and monometallic fragments coordinate the side chains of Arg14 and His15 in 20% ethylene glycol, 0.100 M sodium acetate at pH 4.
View Article and Find Full Text PDFDalton Trans
January 2025
Dipartimento di Farmacia, Università degli Studi "G. D'Annunzio" Chieti-Pescara, Via dei Vestini 31, 66100 Chieti, Italy.
Paddlewheel complexes of bimetallic scaffolds are emerging metallic agents in the bioinorganic chemistry landscape. In the most commonly employed construct, these complexes are decorated by the carboxylate moiety, prompting their possible deployment to target either protein or nucleic acid targets. In this study, density functional investigation was performed to assess viable mechanistic routes for the substitution of one acetate ligand with one chelating purine, adenine or guanine, in diruthenium and dirhodium tetraacetate paddlewheel complexes.
View Article and Find Full Text PDFTunis Med
March 2024
Pediatric department in Charles Nicolle Hospital, Tunis. Tunisia.
Introduction: Distal renal tubular acidosis (dRTA) is a rare genetic disorder due to the incapacity of the α intercalated cells to excrete protons in the collecting duct. This impaired distal acidification of urine leads to a chronic hyperchloremic metabolic acidosis with a normal plasma anion gap, hypokalemia, and hypercalciuria with hypocitraturia causing nephrocalcinosis. Primary dRTA is inherited either as an autosomal dominant (SLC1A4 gene) or autosomal recessive trait (ATP6V0A1/ATP6V1B1 genes).
View Article and Find Full Text PDFBiochem Biophys Res Commun
March 2024
Department of Cell Biology, Oita University Faculty of Medicine, Yufu, Oita, Japan. Electronic address:
V-ATPase is an ATP hydrolysis-driven proton pump involved in the acidification of intracellular organelles and systemic acid-base homeostasis through H secretion in the renal collecting ducts. V-ATPase dysfunction is associated with hereditary distal renal tubular acidosis (dRTA). ATP6V1B1 encodes the B1 subunit of V-ATPase that is integral to ATP hydrolysis and subsequent H transport.
View Article and Find Full Text PDFActa Med Indones
October 2023
1. Department of Internal Medicine, Faculty of Medicine, University of Mataram - West Nusa Tenggara General Hospital, Mataram, Indonesia. 2. Fellow of Nephrology and Hypertension, Department of Internal Medicine, Faculty of Medicine Universitas Indonesia - Cipto Mangunkusumo National Hospital, Jakar
Hypokalemia due to loss of potassium through the kidneys can be caused by distal Renal Tubular Acidosis (dRTA). The etiology of dRTA can be primary due to genetic defects or secondary to autoimmune diseases, especially Sjogren's syndrome (SS). The occurrence of dRTA in SS patients is low, at only 5% of cases.
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