Interaction of cisplatin with a CCHC zinc finger motif‡. (19th February 2013)
- Record Type:
- Journal Article
- Title:
- Interaction of cisplatin with a CCHC zinc finger motif‡. (19th February 2013)
- Main Title:
- Interaction of cisplatin with a CCHC zinc finger motif‡
- Authors:
- Castiglione Morelli, Maria Antonietta
Ostuni, Angela
Cristinziano, Pier Luigi
Tesauro, Diego
Bavoso, Alfonso - Other Names:
- Morelli Giancarlo guestEditor.
- Abstract:
- Abstract : The interaction between cisplatin and an 18‐residue CCHC zinc finger motif derived from a retroviral nucleocapsid protein (PyrZf18) has been studied using UV–visible, CD and 1 H NMR spectroscopies and ESI‐MS spectrometry. Cisplatin irreversibly blocks the cysteine zinc binding groups in the free peptide and is able to slowly eject zinc from the zinc–peptide complex. The observed end product of the reaction with cisplatin is a complex in which only one ammonia molecule is coordinated to platinum. After an initial binding with two cysteine residues and the formation of the (PyrZf18)–platinum–(NH3 )2 complex, a release of one ammonia molecule occurs because of trans ‐labilization, and the third cysteine is coordinated, leading to a mixture of isomers and/or conformers of the (PyrZf18)–platinum–NH3 complex. The results are discussed with respect to the potential antiretroviral activity of platinum(II) compounds and to the possible interaction of cisplatin with the cellular nucleic acid binding proteins. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd. Abstract : This study is focused on the interaction between cisplatin and an 18‐residue CCHC zinc finger motif derived from a retroviral nucleocapsid protein (PyrZf18) UV–visible, CD and 1 H NMR spectroscopies and ESI‐MS spectrometry. The results are discussed with respect to the potential antiretroviral activity of platinum(II) compounds and to the possible interaction of cisplatin with the cellularAbstract : The interaction between cisplatin and an 18‐residue CCHC zinc finger motif derived from a retroviral nucleocapsid protein (PyrZf18) has been studied using UV–visible, CD and 1 H NMR spectroscopies and ESI‐MS spectrometry. Cisplatin irreversibly blocks the cysteine zinc binding groups in the free peptide and is able to slowly eject zinc from the zinc–peptide complex. The observed end product of the reaction with cisplatin is a complex in which only one ammonia molecule is coordinated to platinum. After an initial binding with two cysteine residues and the formation of the (PyrZf18)–platinum–(NH3 )2 complex, a release of one ammonia molecule occurs because of trans ‐labilization, and the third cysteine is coordinated, leading to a mixture of isomers and/or conformers of the (PyrZf18)–platinum–NH3 complex. The results are discussed with respect to the potential antiretroviral activity of platinum(II) compounds and to the possible interaction of cisplatin with the cellular nucleic acid binding proteins. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd. Abstract : This study is focused on the interaction between cisplatin and an 18‐residue CCHC zinc finger motif derived from a retroviral nucleocapsid protein (PyrZf18) UV–visible, CD and 1 H NMR spectroscopies and ESI‐MS spectrometry. The results are discussed with respect to the potential antiretroviral activity of platinum(II) compounds and to the possible interaction of cisplatin with the cellular nucleic acid binding proteins. … (more)
- Is Part Of:
- Journal of peptide science. Volume 19:Number 4(2013:Apr.)
- Journal:
- Journal of peptide science
- Issue:
- Volume 19:Number 4(2013:Apr.)
- Issue Display:
- Volume 19, Issue 4 (2013)
- Year:
- 2013
- Volume:
- 19
- Issue:
- 4
- Issue Sort Value:
- 2013-0019-0004-0000
- Page Start:
- 227
- Page End:
- 232
- Publication Date:
- 2013-02-19
- Subjects:
- cisplatin -- CCHC zinc finger -- cellular nucleic acid binding proteins -- retroviral nucleocapsid protein -- 1H NMR -- CD spectroscopy -- ESI‐MS
Peptides -- Periodicals
Peptides -- Periodicals
572.65 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/psc.2490 ↗
- Languages:
- English
- ISSNs:
- 1075-2617
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5030.530000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2118.xml