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6GXJ

X-ray structure of DiRu-1-encapsulated Apoferritin

Summary for 6GXJ
Entry DOI10.2210/pdb6gxj/pdb
Related5ERK
DescriptorFerritin light chain, CADMIUM ION, CHLORIDE ION, ... (6 entities in total)
Functional Keywordsmetal transport, metal-based compound encapsulation, ruthenium complex, ferritin nanocage
Biological sourceEquus caballus (Horse)
Total number of polymer chains1
Total formula weight21347.69
Authors
Pica, A.,Ferraro, G.,Merlino, A. (deposition date: 2018-06-27, release date: 2019-02-06, Last modification date: 2024-01-17)
Primary citationPetruk, G.,Monti, D.M.,Ferraro, G.,Pica, A.,D'Elia, L.,Pane, F.,Amoresano, A.,Furrer, J.,Kowalski, K.,Merlino, A.
Encapsulation of the Dinuclear Trithiolato-Bridged Arene Ruthenium Complex Diruthenium-1 in an Apoferritin Nanocage: Structure and Cytotoxicity.
ChemMedChem, 14:594-602, 2019
Cited by
PubMed Abstract: The effects of encapsulating the cytotoxic dinuclear trithiolato-bridged arene ruthenium complex [(η -p-MeC H iPr) Ru (μ -S-p-C H tBu) ]Cl (DiRu-1) within the apoferritin (AFt) nanocage were investigated. The DiRu-1-AFt nanocarrier was characterized by UV/Vis spectroscopy, ICP-MS, CD and X-ray crystallography. In contrast to previously reported Au- and Pt-based drug-loaded AFt carriers, we found no evidence of direct interactions between DiRu-1 and AFt. DiRu-1-AFt is cytotoxic toward immortalized murine BALB/c-3T3 fibroblasts transformed with SV40 virus (SVT2) and human epidermoid carcinoma A431 malignant cells, and exhibits moderate selectivity for these cancer cells over normal BALB/c-3T3 cells. DiRu-1-AFt triggers the production of reactive oxygen species, depolarization of mitochondrial membrane potential, and induces cell death via p53-mediated apoptosis. Comparison between our data and previous results suggests that the presence of specific interactions between a metal-based drug and AFt within the protein cage is not essential for drug encapsulation.
PubMed: 30674089
DOI: 10.1002/cmdc.201800805
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.43 Å)
Structure validation

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