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Site-Selective Artificial Ribonucleases: Renaissance of Oligonucleotide Conjugates for Irreversible Cleavage of RNA Sequences
| Content Provider | MDPI |
|---|---|
| Author | Staroseletz, Yaroslav Gaponova, Svetlana Patutina, Olga Bichenkova, Elena Amirloo, Bahareh Heyman, Thomas Chiglintseva, Daria Zenkova, Marina |
| Copyright Year | 2021 |
| Description | RNA-targeting therapeutics require highly efficient sequence-specific devices capable of RNA irreversible degradation in vivo. The most developed methods of sequence-specific RNA cleavage, such as siRNA or antisense oligonucleotides (ASO), are currently based on recruitment of either intracellular multi-protein complexes or enzymes, leaving alternative approaches (e.g., ribozymes and DNAzymes) far behind. Recently, site-selective artificial ribonucleases combining the oligonucleotide recognition motifs (or their structural analogues) and catalytically active groups in a single molecular scaffold have been proven to be a great competitor to siRNA and ASO. Using the most efficient catalytic groups, utilising both metal ion-dependent (Cu(II)-2,9-dimethylphenanthroline) and metal ion-free (Tris(2-aminobenzimidazole)) on the one hand and PNA as an RNA recognising oligonucleotide on the other, allowed site-selective artificial RNases to be created with half-lives of 0.5–1 h. Artificial RNases based on the catalytic peptide [(ArgLeu)2Gly]2 were able to take progress a step further by demonstrating an ability to cleave miRNA-21 in tumour cells and provide a significant reduction of tumour growth in mice. |
| Starting Page | 1732 |
| e-ISSN | 14203049 |
| DOI | 10.3390/molecules26061732 |
| Journal | Molecules |
| Issue Number | 6 |
| Volume Number | 26 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2021-03-19 |
| Access Restriction | Open |
| Subject Keyword | Molecules Biochemistry and Molecular Biology Artificial Ribonuclease Oligonucleotide-peptide Conjugate Rna Cleavage Neocuproine Tris(2-aminobenzimidazole) Pnazyme Mirnase |
| Content Type | Text |
| Resource Type | Article |
