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Expanding the chemical nature of siRNAs: Oxaliplatin as metalation reagent.

Sykfont Snygg, Åse LU and Elmroth, Sofi LU (2009) In Biochemical and Biophysical Research Communications 379(2). p.186-190
Abstract
Short interfering RNAs (siRNAs) can down-regulate protein production by site specific degradation of mRNA. We here report the in vitro efficiency of three siRNAs metalated with oxaliplatin. All siRNAs were selectively platinated in the sense strand, and designed to target the AU-rich 3' UTR region of Wnt-5a mRNA cloned into a luciferase reporter plasmid. Two of the studied siRNAs reveal luciferase protein suppression levels well above 90% when used in nano-molar concentrations for both metalated and the corresponding native siRNA. The platinated siRNAs were also characterized with respect to thermal melting properties, and the number of platinum adducts on the different sense strands were determined by MALDI-ToF MS. In all cases,... (More)
Short interfering RNAs (siRNAs) can down-regulate protein production by site specific degradation of mRNA. We here report the in vitro efficiency of three siRNAs metalated with oxaliplatin. All siRNAs were selectively platinated in the sense strand, and designed to target the AU-rich 3' UTR region of Wnt-5a mRNA cloned into a luciferase reporter plasmid. Two of the studied siRNAs reveal luciferase protein suppression levels well above 90% when used in nano-molar concentrations for both metalated and the corresponding native siRNA. The platinated siRNAs were also characterized with respect to thermal melting properties, and the number of platinum adducts on the different sense strands were determined by MALDI-ToF MS. In all cases, platination was accompanied by a decrease in melting temperature. Further, the dominating oxaliplatin metalation site was the r(GpG)-adduct. The study indicates that metalation can be used as a general strategy to further expand the chemical nature of siRNAs. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
379
issue
2
pages
186 - 190
publisher
Elsevier
external identifiers
  • wos:000262924300005
  • pmid:19109929
  • scopus:58249109705
ISSN
1090-2104
DOI
10.1016/j.bbrc.2008.12.068
language
English
LU publication?
yes
id
6b55f040-335e-4420-a57f-6dd2199330e7 (old id 1275912)
date added to LUP
2009-01-29 16:04:37
date last changed
2017-01-01 05:28:18
@article{6b55f040-335e-4420-a57f-6dd2199330e7,
  abstract     = {Short interfering RNAs (siRNAs) can down-regulate protein production by site specific degradation of mRNA. We here report the in vitro efficiency of three siRNAs metalated with oxaliplatin. All siRNAs were selectively platinated in the sense strand, and designed to target the AU-rich 3' UTR region of Wnt-5a mRNA cloned into a luciferase reporter plasmid. Two of the studied siRNAs reveal luciferase protein suppression levels well above 90% when used in nano-molar concentrations for both metalated and the corresponding native siRNA. The platinated siRNAs were also characterized with respect to thermal melting properties, and the number of platinum adducts on the different sense strands were determined by MALDI-ToF MS. In all cases, platination was accompanied by a decrease in melting temperature. Further, the dominating oxaliplatin metalation site was the r(GpG)-adduct. The study indicates that metalation can be used as a general strategy to further expand the chemical nature of siRNAs.},
  author       = {Sykfont Snygg, Åse and Elmroth, Sofi},
  issn         = {1090-2104},
  language     = {eng},
  number       = {2},
  pages        = {186--190},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Expanding the chemical nature of siRNAs: Oxaliplatin as metalation reagent.},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2008.12.068},
  volume       = {379},
  year         = {2009},
}