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Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives
In recent years, RNA has gained traction both as a therapeutic molecule and as a therapeutic target in several human pathologies. In this review, we consider the approach of targeting RNA using small molecules for both research and therapeutic purposes. Given the primary challenge presented by the l...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10687564/ https://www.ncbi.nlm.nih.gov/pubmed/38033386 http://dx.doi.org/10.3389/fmolb.2023.1298441 |
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author | Li, Aixiao Bouhss, Ahmed Clément, Marie-Jeanne Bauvais, Cyril Taylor, J. Paul Bollot, Guillaume Pastré, David |
author_facet | Li, Aixiao Bouhss, Ahmed Clément, Marie-Jeanne Bauvais, Cyril Taylor, J. Paul Bollot, Guillaume Pastré, David |
author_sort | Li, Aixiao |
collection | PubMed |
description | In recent years, RNA has gained traction both as a therapeutic molecule and as a therapeutic target in several human pathologies. In this review, we consider the approach of targeting RNA using small molecules for both research and therapeutic purposes. Given the primary challenge presented by the low structural diversity of RNA, we discuss the potential for targeting RNA: protein interactions to enhance the structural and sequence specificity of drug candidates. We review available tools and inherent challenges in this approach, ranging from adapted bioinformatics tools to in vitro and cellular high-throughput screening and functional analysis. We further consider two critical steps in targeting RNA/protein interactions: first, the integration of in silico and structural analyses to improve the efficacy of molecules by identifying scaffolds with high affinity, and second, increasing the likelihood of identifying on-target compounds in cells through a combination of high-throughput approaches and functional assays. We anticipate that the development of a new class of molecules targeting RNA: protein interactions to prevent physio-pathological mechanisms could significantly expand the arsenal of effective therapeutic compounds. |
format | Online Article Text |
id | pubmed-10687564 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-106875642023-11-30 Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives Li, Aixiao Bouhss, Ahmed Clément, Marie-Jeanne Bauvais, Cyril Taylor, J. Paul Bollot, Guillaume Pastré, David Front Mol Biosci Molecular Biosciences In recent years, RNA has gained traction both as a therapeutic molecule and as a therapeutic target in several human pathologies. In this review, we consider the approach of targeting RNA using small molecules for both research and therapeutic purposes. Given the primary challenge presented by the low structural diversity of RNA, we discuss the potential for targeting RNA: protein interactions to enhance the structural and sequence specificity of drug candidates. We review available tools and inherent challenges in this approach, ranging from adapted bioinformatics tools to in vitro and cellular high-throughput screening and functional analysis. We further consider two critical steps in targeting RNA/protein interactions: first, the integration of in silico and structural analyses to improve the efficacy of molecules by identifying scaffolds with high affinity, and second, increasing the likelihood of identifying on-target compounds in cells through a combination of high-throughput approaches and functional assays. We anticipate that the development of a new class of molecules targeting RNA: protein interactions to prevent physio-pathological mechanisms could significantly expand the arsenal of effective therapeutic compounds. Frontiers Media S.A. 2023-11-16 /pmc/articles/PMC10687564/ /pubmed/38033386 http://dx.doi.org/10.3389/fmolb.2023.1298441 Text en Copyright © 2023 Li, Bouhss, Clément, Bauvais, Taylor, Bollot and Pastré. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Li, Aixiao Bouhss, Ahmed Clément, Marie-Jeanne Bauvais, Cyril Taylor, J. Paul Bollot, Guillaume Pastré, David Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title | Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title_full | Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title_fullStr | Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title_full_unstemmed | Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title_short | Using the structural diversity of RNA: protein interfaces to selectively target RNA with small molecules in cells: methods and perspectives |
title_sort | using the structural diversity of rna: protein interfaces to selectively target rna with small molecules in cells: methods and perspectives |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10687564/ https://www.ncbi.nlm.nih.gov/pubmed/38033386 http://dx.doi.org/10.3389/fmolb.2023.1298441 |
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