Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum (783 views)
Oncology Research (ISSN: 0965-0407), 2003; 13(5): 279-287.
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Paper type: Journal Article,
Impact factor: 1.794, 5-year impact factor: 1.193
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0842305853&partnerID=40&md5=10517ce6415c4947d843c73d317532fd
Keywords: Decoy, Peptide Nucleic Acid (pna), Peptide Nucleic Acid (pna)-Dna Chimeras, Cell Extract, Endonuclease, Exonuclease, Immunoglobulin Enhancer Binding Protein, Liposome, Protein P50, Transcription Factor, Transcription Factor Decoy, Transcription Factor Sp1, Unclassified Drug, Exodeoxyribonuclease, Oligonucleotide, Phosphatase, Article, Binding Site, Cancer Invasion, Controlled Study, Dna Binding, Dna Flanking Region, Enzyme Activity, Enzyme Degradation, Gene Targeting, Human, Human Cell, In Vitro Study, In Vivo Study, Priority Journal, Protein Localization, Tumor Growth, Animal, Blood, Cattle, Cell Line, Chemistry, Dose Response, Enzyme Activation, Metabolism, Physiology, Dose-Response Relationship, Phosphoric Monoester Hydrolases,
Affiliations:
*** IBB - CNR ***
Dept. of Biochem. and Molec. Biology, Ferrara University, Ferrara, Italy
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Dept. Pharmaceut. Chem. and Technol., University of Perugia, Perugia, Italy
Biotechnology Center, Ferrara University, Ferrara, Italy
Dipto. di Biochim. e Biol. Molec., Via L. Borsari n.46, 44100 Ferrara, Italy
References:
Not available.
Oncology Research (ISSN: 0965-0407), 2003; 13(5): 279-287.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.794, 5-year impact factor: 1.193
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0842305853&partnerID=40&md5=10517ce6415c4947d843c73d317532fd
Keywords: Decoy, Peptide Nucleic Acid (pna), Peptide Nucleic Acid (pna)-Dna Chimeras, Cell Extract, Endonuclease, Exonuclease, Immunoglobulin Enhancer Binding Protein, Liposome, Protein P50, Transcription Factor, Transcription Factor Decoy, Transcription Factor Sp1, Unclassified Drug, Exodeoxyribonuclease, Oligonucleotide, Phosphatase, Article, Binding Site, Cancer Invasion, Controlled Study, Dna Binding, Dna Flanking Region, Enzyme Activity, Enzyme Degradation, Gene Targeting, Human, Human Cell, In Vitro Study, In Vivo Study, Priority Journal, Protein Localization, Tumor Growth, Animal, Blood, Cattle, Cell Line, Chemistry, Dose Response, Enzyme Activation, Metabolism, Physiology, Dose-Response Relationship, Phosphoric Monoester Hydrolases,
Affiliations:
*** IBB - CNR ***
Dept. of Biochem. and Molec. Biology, Ferrara University, Ferrara, Italy
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Dept. Pharmaceut. Chem. and Technol., University of Perugia, Perugia, Italy
Biotechnology Center, Ferrara University, Ferrara, Italy
Dipto. di Biochim. e Biol. Molec., Via L. Borsari n.46, 44100 Ferrara, Italy
References:
Not available.
Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum
Double-stranded molecules based on peptide nucleic acids (PNAs)-DNA chimeras carrying binding sites for known transcription factors could be of great interest in decoy pharmacotherapy of neoplastic diseases. For instance, decoy molecules recognizing Sp1 and NF-kappaB transcription factors were found to inhibit tumor cell growth and invasion activity. In this respect, we have recently found that double-stranded PNA-DNA chimeras carrying NF-kappaB binding sites inhibit the binding of NF-kappaB p52 and p50 transcription factors to target DNA molecules. In this article we determined the resistance of double-stranded decoy molecules based on PNA-DNA chimeras to exonucleases (both 3'-->5' and 5'-->3' exonucleases), endonucleases, and 5'-phosphatases. In addition, we performed experiments aimed at determining the resistance of these molecules in cellular extracts and serum. Finally, we used liposomes as protective agents in experimental conditions in which the decoy molecules employed were found to be unstable (high concentrations of enzymes, cellular extracts, or serum). The results obtained demonstrated that decoy molecules based on PNA-DNA chimeras are more resistant than DNA-based decoys to exo- and endonucleases, serum, and cellular extracts. In addition, the resistance of DNA/PNA hybrids in the presence of high concentrations of serum and cellular extracts was increased after complexation to cationic liposomes, due to the fact that double-stranded PNA-DNA-PNA chimeras bind to these delivery systems. The results obtained in the present study support the proposal of molecules based on PNA-DNA chimeras for an efficient decoy treatment of tumor cells both in vitro and in vivo.
Double-stranded molecules based on peptide nucleic acids (PNAs)-DNA chimeras carrying binding sites for known transcription factors could be of great interest in decoy pharmacotherapy of neoplastic diseases. For instance, decoy molecules recognizing Sp1 and NF-kappaB transcription factors were found to inhibit tumor cell growth and invasion activity. In this respect, we have recently found that double-stranded PNA-DNA chimeras carrying NF-kappaB binding sites inhibit the binding of NF-kappaB p52 and p50 transcription factors to target DNA molecules. In this article we determined the resistance of double-stranded decoy molecules based on PNA-DNA chimeras to exonucleases (both 3'-->5' and 5'-->3' exonucleases), endonucleases, and 5'-phosphatases. In addition, we performed experiments aimed at determining the resistance of these molecules in cellular extracts and serum. Finally, we used liposomes as protective agents in experimental conditions in which the decoy molecules employed were found to be unstable (high concentrations of enzymes, cellular extracts, or serum). The results obtained demonstrated that decoy molecules based on PNA-DNA chimeras are more resistant than DNA-based decoys to exo- and endonucleases, serum, and cellular extracts. In addition, the resistance of DNA/PNA hybrids in the presence of high concentrations of serum and cellular extracts was increased after complexation to cationic liposomes, due to the fact that double-stranded PNA-DNA-PNA chimeras bind to these delivery systems. The results obtained in the present study support the proposal of molecules based on PNA-DNA chimeras for an efficient decoy treatment of tumor cells both in vitro and in vivo.
Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum
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Resistance of decoy PNA-DNA chimeras to enzymatic degradation in cellular extracts and serum
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View Export to BibTeX Export to EndNote
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Impact Factor: 4.803
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 1.567
View Export to BibTeX Export to EndNote
Menchise V, De Simone G, Tedeschi T, Corradini R, Sforza S, Marchelli R, Capasso D, Saviano M, Pedone C
* Insights into peptide nucleic acid (PNA) structural features: The crystal structure of a D-lysine-based chiral PNA-DNA duplex (2747 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2003 Oct 14; 100(21): 12021-12026.
Impact Factor: 10.272
View Export to BibTeX Export to EndNote
Borgatti M, Lampronti I, Romanelli A, Pedone C, Saviano M, Bianchi N, Mischiati C, Gambari R
* Transcription factor decoy molecules based on a peptide nucleic acid (PNA)-DNA chimera mimicking Sp1 binding sites (1319 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2003 Feb 28; 278(9): 7500-7509.
Impact Factor: 6.482
View Export to BibTeX Export to EndNote
Borgatti M, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Mischiati C, Pedone C, Gambari R
* Cationic Liposomes As Delivery Systems For Double-Stranded Pna-Dna Chimeras Exhibiting Decoy Activity Against Nf-Kappab Transcription Factors (851 views)
Biochem Pharmacol Biochemical Pharmacology (ISSN: 1873-2968, 0006-2952), 2002 Sep 15; 64(4): 609-616.
Impact Factor: 3.542
View Export to BibTeX Export to EndNote
14 Records (13 excluding Abstracts).
Total impact factor: 63.207 (61.393 excluding Abstracts).
Total 5 year impact factor: 66.097 (64.278 excluding Abstracts).
Total impact factor: 63.207 (61.393 excluding Abstracts).
Total 5 year impact factor: 66.097 (64.278 excluding Abstracts).
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