Gold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins, 1st ed. 2018
Springer Theses Series

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Language: English

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Gold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins
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151 p. · 15.5x23.5 cm · Paperback

Approximative price 105.49 €

In Print (Delivery period: 15 days).

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Gold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins
Publication date:
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This book examines Au (I, III) complexes that selectively attack and inhibit zinc finger proteins (ZnFs) for potential therapeutic use. The author explores gold(I)-phosphine, gold(III) complexes with N^N and C^N donors as inhibitors of the HIV-1 nucleocapsid protein (NCp7), in comparison to the human transcription factor Sp1. To determine the coordination sphere of the gold adducts formed by interaction with ZnFs, two innovative approaches are used, based on Travelling-Wave Ion Mobility coupled with Mass Spectrometry (TWIM-MS), and X-ray Absorption Spectroscopy. Both approaches are proven to yield valuable structural information regarding the coordination sphere of gold in the adducts. In addition, the organometallic compound [Au (bnpy)Cl2] is evaluated. The system is shown to be capable of inhibiting ZnFs by means of C?S coupling.

Au(I)-phosphine series design.- Probing the Protein: Ion Mobility Spectrometry.- Probing Gold: X-ray Absorption Spectroscopy.- Probing Cells: Cytotoxicity Evaluation.- Au(III) series with k2C,N and k2N,N' ligands.- "Dual Probe" X-ray Absorption Spectroscopy.

Nominated as an outstanding Ph.D. thesis by the University of Campinas, Brazil

Presents an innovative approach, using gold chemistry to target zinc finger proteins

Explores the use of Travelling-Wave Ion Mobility coupled with Mass Spectrometry, and X-ray Absorption Spectroscopy to obtain structural information on the Gold adducts