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@ARTICLE{Calandrini:201334,
author = {Calandrini, Vania and Nguyen, Trung Hai and Arnesano, Fabio
and Galliani, Angela and Ippoliti, Emiliano and Carloni,
Paolo and Natile, Giovanni},
title = {{S}tructural {B}iology of {C}isplatin {C}omplexes with
{C}ellular {T}argets: {T}he {A}dduct with {H}uman {C}opper
{C}haperone {A}tox1 in {A}queous {S}olution},
journal = {Chemistry - a European journal},
volume = {20},
number = {37},
issn = {0947-6539},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2015-03631},
pages = {11719 - 11725},
year = {2014},
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.},
cin = {INM-9 / IAS-5 / GRS},
ddc = {540},
cid = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330 /
I:(DE-Juel1)GRS-20100316},
pnm = {899 - ohne Topic (POF2-899)},
pid = {G:(DE-HGF)POF2-899},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000341630500019},
pubmed = {pmid:25111319},
doi = {10.1002/chem.201402834},
url = {https://juser.fz-juelich.de/record/201334},
}