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Syntheses and evaluation of drug-like properties of CO-releasing molecules containing ruthenium and group 6 metal. | LitMetric

AI Article Synopsis

  • - The paper examines the drug-like properties of various carbonyl metal CO-releasing molecules, focusing on their cytotoxicity, in vivo toxicity, bio-distribution, and metabolism through a series of experiments.
  • - Cytotoxic tests revealed a range of effective concentrations (IC₅₀ values) for different complexes, with some complexes exhibiting significant toxicity at specific dosages in mice, leading to observable liver and kidney damage after repeated administration.
  • - Analysis showed uneven distribution of the compounds in different tissues, and it was found that the metal ions within the complexes could be oxidized or remain in their original state during metabolic processes.

Article Abstract

In this paper, drug-like properties of two series of carbonyl metal CO-releasing molecules, Ru(CO)₃Cl(n)L (n=1, L=amino acid or its derivatives 1-7, L=acetylacetone 8 or 2,2'-bipyridyl 9; n=2, L=aminopyridine derivatives 10-13; n=0, L=salicylaldehyde Schiff base 14-15) and M(CO)₅L(M=Cr, Mo, W; L=glycine methyl ester 16-18; L=N-methyl imidazole 19-21), were preliminarily evaluated from four aspects involving in cytotoxicity, in vivo toxicity, bio-distribution and metabolism. Cytotoxic effects of all complexes were assayed by MTT. IC₅₀ values of complexes 1-15 were 39.55-240.16mg/l, and those of complexes 16 and 18 were 21.36-22.21 mg/l. Toxicity tests of mice used oral acute toxic class method and got LD₅₀ values of some complexes; among them, LD₅₀ of complex 1 was in 800-1000 mg/kg, complex 7 in 1100-1500 mg/kg and complex 18 in 75-125 mg/kg. After several consecutive administrations, tested complexes severely damaged liver and kidney in both functional and morphological aspects. And by metal ions measurements using ICP-AES, we found that the tested complexes were unevenly distributed in tissues and organs. In vivo, Ru(II) in complexes was oxidized to Ru(III) by P450 enzymes, and for Mo(0) and W(0) in complexes, part of them transformed into higher oxidation state, the others kept original state.

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http://dx.doi.org/10.1016/j.ejmech.2013.12.041DOI Listing

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