5KJ9

Anticancer activity of Ru- and Os(arene) compounds of a maleimide-functionalized bioactive pyridinecarbothioamide ligand

Summary for 5KJ9

• Entry DOI: 10.2210/pdb5kj9/pdb
• Descriptor: Lysozyme C, SODIUM ION, RUTHENIUM ION, ... (4 entities in total)
• Functional Keywords: lysozyme, anticancer, ligand, ruthenium, hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14455.22

Authors

Sullivan, M.P.,Christian, C.G.,Goldstone, D.C. (deposition date: 2016-06-18, release date: 2016-07-06, Last modification date: 2024-11-20)

Primary citation

Hanif, M.,Moon, S.,Sullivan, M.P.,Movassaghi, S.,Kubanik, M.,Goldstone, D.C.,Sohnel, T.,Jamieson, S.M.,Hartinger, C.G.
Anticancer activity of Ru- and Os(arene) compounds of a maleimide-functionalized bioactive pyridinecarbothioamide ligand.
J. Inorg. Biochem., 165:100-107, 2016

PubMed Abstract: With the aim of increasing the accumulation of Ru anticancer agents in the tumor, a targeted delivery strategy based on a maleimide anchor for the biological vector human serum albumin (HSA) was developed. A group of piano stool Ru- and Os(η-arene) complexes carrying a maleimide-functionalized N-phenyl-2-pyridinecarbothioamide (PCA) ligand was designed allowing for covalent conjugation to biological thiols. The complexes were characterized by NMR spectroscopy, ESI-MS, elemental analysis and single-crystal X-ray diffraction analysis. The compounds were shown to undergo halido/aqua ligand exchange reactions in aqueous solution, depending mainly on the metal center and the nature of the halide. In vitro cytotoxicity studies revealed low potency which is explained by the observed high reactivity of the maleimide to the thiol of l-cysteine (Cys), while the metal center itself shows little affinity to amino acids of the model protein lysozyme.

PubMed: 27470012
DOI: 10.1016/j.jinorgbio.2016.06.025

Experimental method

X-RAY DIFFRACTION (1.2 Å)