Fluorescent sensors have been widely used as microscopic tools to image Zn2+ on a cellular level. TSQ and Zinquin make adducts with Zn-proteins and have been used to image Zn-proteome. If TSQ and Zinquin bind specifically to many Zn-proteins; it is hypothesized that other metal binding ligands, both synthetic and natural, may also bind to the Zn-proteome. Biologically active 1,10-phenanthroline and related molecules were investigated for their ability to bind to Zn-proteome. Similarly, cellular glutathione was investigated. In our study, it has been seen that, 1,10-phenanthroline and some other metal binding bidentate ligands, were able to displace TSQ from TSQ-Zn-proteome. Specifically when cellular Zn-proteome reacted with TSQ, adduct formation occurs; that is detected by fluorescence emission at 470 nm. Upon reaction of TSQ-Zn-proteome with 1,10-phenanthroline, glutathione, or some other related small molecules, a significant decrease in fluorescence was observed, indicating the displacement of TSQ. NSDS PAGE electrophoresis of the product solution further confirmed the displacement of TSQ from an array of Zn-proteins.

Reaction of zinc proteome with biologically important metal binding ligands

248th National Meeting (2014)

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