Journal Article

FZJ-2015-03631

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural Biology of Cisplatin Complexes with Cellular Targets: The Adduct with Human Copper Chaperone Atox1 in Aqueous Solution

Calandrini, V.FZJ* ; Nguyen, T. H.GRS* ; Arnesano, F. ; Galliani, A. ; Ippoliti, E.FZJ* ; Carloni, P. (Corresponding Author)FZJ* ; Natile, G.

2014
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/chem.201402834

Abstract: Cisplatin is one of the most used anticancer drugs. Its cellular influx and delivery to target DNA may involve the copper chaperone Atox1 protein. Although the mode of binding is established by NMR spectroscopy measurements in solution—the Pt atom binds to Cys12 and Cys15 while retaining the two ammine groups—the structural determinants of the adduct are not known. Here a structural model by hybrid Car–Parrinello density functional theory-based QM/MM simulations is provided. The platinated site minimally modifies the fold of the protein. The calculated NMR and CD spectral properties are fully consistent with the experimental data. Our in silico/in vitro approach provides, together with previous studies, an unprecedented view into the structural biology of cisplatin–protein adducts.

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Contributing Institute(s):

1. Computational Biomedicine (INM-9)
2. Computational Biomedicine (IAS-5)
3. GRS (GRS)

Research Program(s):

1. 899 - ohne Topic (POF2-899) (POF2-899)

Appears in the scientific report 2015

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Database coverage:
; Current Contents - Physical, Chemical and Earth Sciences ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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