Abstract
The interaction of cis-DDP and trans-DDP (DDP=[PtCl2(NH3)2]) with the C-terminal zinc finger (ZF2) of the HIVNCp7 nucleocapsid protein was investigated by fluorescence, circular dichroism, mass spectrometry, and {1H, 15N} HSQC (heteronuclear single quantum coherence) NMR spectroscopy. The rate of reaction differed significantly for the two compounds, with the trans isomer reacting in a significantly faster manner, as expected. {1H, 15N} HSQC NMR of 15N-labeled compounds with the ZF2 showed the appearance of several new 15N peaks, consistent with sulfur binding and formation of Pt-S species. Mass spectrometry confirmed the formation of several different Pt-apopeptide/ZF2 adducts. Circular dichroism and fluorescence spectroscopy also indicated conformational changes upon binding while a 33% decrease in fluorescence of the unique tryptophan residue was seen in 72h upon complexation of the cis isomer, while the trans isomer quenched 50% in just 24h.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
