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Updated: Feb 16, 2026

Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
Selective targeting of PARP-1 zinc finger recognition domains with Au(iii) organometallics
Margot N Wenzel1, Samuel M Meier-Menches, Thomas L Williams
1School of Chemistry, Cardiff University, Main Building, Park Place, CF10 3AT Cardiff, UK. casinia@cardiff.ac.uk.
Abstract:
The binding of Au(iii) complexes to the zinc finger domain of the anticancer drug target PARP-1 was studied using a hyphenated mass spectrometry approach combined with quantum mechanics/molecular mechanics (QM/MM) studies. Competition experiments were carried out, whereby each Au complex was exposed to two types of zinc fingers. Notably, the cyclometallated Au-C^N complex was identified as the most selective candidate to disrupt the PARP-1 zinc finger domain, forming distinct adducts compared to the coordination compound Auphen.
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