Please use this identifier to cite or link to this item:
Title: Simultaneous mass spectrometry analysis of cisplatin with oligonucleotide-peptide mixtures: implications for the mechanism of action
Authors: Mansouri, Farangis
Patiny, Luc
Ortiz, Daniel
Menin, Laure
Davey, Curtis Alexander
Mohammadi, Fakhrossadat
Dyson, Paul J.
Keywords: Science::Biological sciences
Issue Date: 2022
Source: Mansouri, F., Patiny, L., Ortiz, D., Menin, L., Davey, C. A., Mohammadi, F. & Dyson, P. J. (2022). Simultaneous mass spectrometry analysis of cisplatin with oligonucleotide-peptide mixtures: implications for the mechanism of action. JBIC Journal of Biological Inorganic Chemistry, 27(2), 239-248.
Project: 2020-T1-001-128 
Journal: JBIC Journal of Biological Inorganic Chemistry 
Abstract: Although genomic DNA is the primary target of anticancer platinum-based drugs, interactions with proteins also play a significant role in their overall activity. In this study, competitive binding of cisplatin with an oligonucleotide and two peptides corresponding to segments of H2A and H2B histone proteins was investigated by mass spectrometry. Following the determination of the cisplatin binding sites on the oligonucleotide and peptides by tandem mass spectrometry, competitive binding was studied and transfer of platinum fragments from the platinated peptides to the oligonucleotide explored. In conjunction with previous studies on the nucleosome, the results suggest that all four of the abundant histone proteins serve as a platinum drug reservoir in the cell nucleus, providing an adduct pool that can be ultimately transferred to the DNA.
ISSN: 0949-8257
DOI: 10.1007/s00775-022-01924-9
Schools: School of Biological Sciences 
Research Centres: NTU Institute of Structural Biology
Rights: © The Author(s) 2022. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
s00775-022-01924-9.pdf900.35 kBAdobe PDFThumbnail

Citations 50

Updated on Dec 3, 2023

Web of ScienceTM
Citations 50

Updated on Oct 25, 2023

Page view(s)

Updated on Dec 7, 2023


Updated on Dec 7, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.