Interaction of cisplatin with human superoxide dismutase

Lucia Banci, Ivano Bertini, Olga Blaževitš, Vito Calderone, Francesca Cantini, Jiafei Mao, Angela Trapananti, Miguela Vieru, Ilaria Amori, Mauro Cozzolino, Maria Teresa Carrì

Research output: Contribution to journalArticlepeer-review

Abstract

cis-Diamminedichloroplatinum(II) (cisplatin) is able to interact with human superoxide dismutase (hSOD1) in the disulfide oxidized apo form with a dissociation constant of 37 ± 3 μM through binding cysteine 111 (Cys111) located at the edge of the subunit interface. It also binds to Cu 2-Zn 2 and Zn 2-Zn 2 forms of hSOD1. Cisplatin inhibits aggregation of demetalated oxidized hSOD1, and it is further able to dissolve and monomerize oxidized hSOD1 oligomers in vitro and in cell, thus indicating its potential as a leading compound for amyotrophic lateral sclerosis.

Original languageEnglish
Pages (from-to)7009-7014
Number of pages6
JournalJournal of the American Chemical Society
Volume134
Issue number16
DOIs
Publication statusPublished - Apr 25 2012

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

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