ArticleNucleic acids research2020
Strict conformational demands of RNA cleavage in bulge-loops created by peptidyl-oligonucleotide conjugates.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- A Bifunctional Small Molecule Degrader of the Long Noncoding RNA MALAT1 Triplex.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Click Conjugates of Artificial Ribonucleases: Sequence Specific Cleavage with Multiple Turnover.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Opening new frontiers with catalytic nucleic acids in miRNA inhibition.Frontiers in pharmacology · 2025Review
- Bulge-Forming miRNases Cleave Oncogenic miRNAs at the Central Loop Region in a Sequence-Specific Manner.International journal of molecular sciences · 2022Article
- Influence of sequence variation on the RNA cleavage activity of ZnRSC advances · 2022Article
- "Bind, cleave and leave": multiple turnover catalysis of RNA cleavage by bulge-loop inducing supramolecular conjugates.Nucleic acids research · 2022Article
- Innovative developments and emerging technologies in RNA therapeutics.RNA biology · 2022Article
- Site-Selective Artificial Ribonucleases: Renaissance of Oligonucleotide Conjugates for Irreversible Cleavage of RNA Sequences.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potent knockdown of pathogenic RNA in vivo is an urgent health need unmet by both small-molecule and biologic drugs. 'Smart' supramolecular assembly of catalysts offers precise recognition and potent destruction of targeted RNA, hitherto not found in nature. Peptidyl-oligonucleotide ribonucleases are here chemically engineered to create and attack bulge-loop regions upon hybridization to target RNA. Catalytic peptide was incorporated either via a centrally modified nucleotide (Type 1) or through an abasic sugar residue (Type 2) within the RNA-recognition motif to reveal striking differences in biological performance and strict structural demands of ribonuclease activity. None of the Type 1 conjugates were catalytically active, whereas all Type 2 conjugates cleaved RNA target in a sequence-specific manner, with up to 90% cleavage from 5-nt bulge-loops (BC5-α and BC5L-β anomers) through multiple cuts, including in folds nearby. Molecular dynamics simulations provided structural explanation of accessibility of the RNA cleavage sites to the peptide with adoption of an 'in-line' attack conformation for catalysis. Hybridization assays and enzymatic probing with RNases illuminated how RNA binding specificity and dissociation after cleavage can be balanced to permit turnover of the catalytic reaction. This is an essential requirement for inactivation of multiple copies of disease-associated RNA and therapeutic efficacy.
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