![]()
|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print November 20, 2002
Biochemistry and Molecular Biology, University of Ferrara, Ferrara 44100
Corresponding Author: gam{at}unife.it
Peptide nucleic acids (PNAs) are DNA mimicking molecules in which the sugar-phosphate backbone is replaced by a pseudopeptide backbone composed of N-(2-aminoethyl)glycine units. We determined whether double-stranded molecules based on PNAs and PNA-DNA-PNA (PDP) chimeras could be capable of stable interactions with nuclear proteins belonging to Sp1 transcription factor family and, therefore, could act as decoy reagents able to inhibit molecular interactions between Sp1 and DNA. Since the structure of PNA/PNA hybrids is very different from that of DNA/DNA double helix, they could theoretically alter the molecular structure of the double stranded PNA-DNA-PNA chimeras, perturbing interactions with specific transcription factors. We found that PNA-based hybrids do not inhibit Sp1/DNA interactions. By contrast, hybrid molecules based on PNA-DNA-PNA chimeras are very effective decoy molecules, encouraging further experiments focused on possible use of these molecules for the development of potential agents for a decoy approach in gene therapy. In this respect, the finding that PDP-based decoy molecules are more resistant than DNA/DNA hybrids to enzymatic degradation appears to be of great interest. Furthermore, their resistance can be even improved after complexation with cationic liposomes to which PDP/PDP chimeras are able to bind in virtue of their internal DNA structure.
J. Biol. Chem, 10.1074/jbc.M206780200
Submitted on July 8, 2002
Revised on November 19, 2002
Accepted on November 20, 2002
Transcription factor decoy molecules based on a PNA-DNA chimera mimicking Sp1 binding sites
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
I. Lampronti, M. T.H. Khan, M. Borgatti, N. Bianchi, and R. Gambari Inhibitory Effects of Bangladeshi Medicinal Plant Extracts on Interactions between Transcription Factors and Target DNA Sequences Evid. Based Complement. Altern. Med., September 1, 2008; 5(3): 303 - 312. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Bezzerri, M. Borgatti, E. Nicolis, I. Lampronti, M. C. Dechecchi, I. Mancini, P. Rizzotti, R. Gambari, and G. Cabrini Transcription Factor Oligodeoxynucleotides to NF-{kappa}B Inhibit Transcription of IL-8 in Bronchial Cells Am. J. Respir. Cell Mol. Biol., July 1, 2008; 39(1): 86 - 96. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. C. Dechecchi, E. Nicolis, V. Bezzerri, A. Vella, M. Colombatti, B. M. Assael, Y. Mettey, M. Borgatti, I. Mancini, R. Gambari, et al. MPB-07 Reduces the Inflammatory Response to Pseudomonas aeruginosa in Cystic Fibrosis Bronchial Cells Am. J. Respir. Cell Mol. Biol., May 1, 2007; 36(5): 615 - 624. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Abdelrahim, C. H. Baker, J. L. Abbruzzese, and S. Safe Tolfenamic acid and pancreatic cancer growth, angiogenesis, and Sp protein degradation. J Natl Cancer Inst, June 21, 2006; 98(12): 855 - 868. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Feriotto, A. Finotti, P. Volpe, S. Treves, S. Ferrari, C. Angelelli, F. Zorzato, and R. Gambari Myocyte Enhancer Factor 2 Activates Promoter Sequences of the Human A{beta}H-J-J Locus, Encoding Aspartyl-{beta}-Hydroxylase, Junctin, and Junctate Mol. Cell. Biol., April 15, 2005; 25(8): 3261 - 3275. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Crinelli, M. Bianchi, L. Gentilini, L. Palma, M. D. Sorensen, T. Bryld, R. B. Babu, K. Arar, J. Wengel, and M. Magnani Transcription factor decoy oligonucleotides modified with locked nucleic acids: an in vitro study to reconcile biostability with binding affinity Nucleic Acids Res., March 29, 2004; 32(6): 1874 - 1885. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |