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.

Banci, L., Bertini, I., Blaževitš, O., Calderone, V., Cantini, F., Mao, J., et al. (2012). Interaction of cisplatin with human superoxide dismutase. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 134(16), 7009-7014 [10.1021/ja211591n].

Interaction of cisplatin with human superoxide dismutase

CARRI', MARIA TERESA
2012-04-01

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.
apr-2012
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
superoxide dismutase, cisplatin
Banci, L., Bertini, I., Blaževitš, O., Calderone, V., Cantini, F., Mao, J., et al. (2012). Interaction of cisplatin with human superoxide dismutase. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 134(16), 7009-7014 [10.1021/ja211591n].
Banci, L; Bertini, I; Blaževitš, O; Calderone, V; Cantini, F; Mao, J; Trapananti, A; Vieru, M; Amori, I; Cozzolino, M; Carri', Mt
Articolo su rivista
File in questo prodotto:
File Dimensione Formato  
JACS2012.pdf

solo utenti autorizzati

Licenza: Creative commons
Dimensione 308.93 kB
Formato Unknown
308.93 kB Unknown   Visualizza/Apri   Richiedi una copia

Questo articolo è pubblicato sotto una Licenza Licenza Creative Commons Creative Commons

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/68150
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 64
  • ???jsp.display-item.citation.isi??? 60
social impact