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- Publisher Website: 10.1016/j.cbpa.2023.102334
- Scopus: eid_2-s2.0-85160529067
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Article: Recent advances in the development of peptide-based inhibitors targeting epigenetic readers of histone lysine acetylation and methylation marks
| Title | Recent advances in the development of peptide-based inhibitors targeting epigenetic readers of histone lysine acetylation and methylation marks |
|---|---|
| Authors | |
| Keywords | Chemical probe Epigenetic reader Lysine acetylation Lysine methylation Peptide-based inhibitor |
| Issue Date | 30-May-2023 |
| Publisher | Elsevier |
| Citation | Current Opinion in Chemical Biology, 2023, v. 75 How to Cite? |
| Abstract | Inhibitors for epigenetic readers of histone modifications are useful chemical probes to interrogate the functional roles played by their cognate targets in epigenetic regulation and can even serve as drugs for the treatment of diseases associated with the dysregulated targets. However, many epigenetic readers are intractable to small molecules, as the recognition of modified histone peptides commonly involves flat and extended protein surfaces. In contrast, the relatively large sizes and structural complexity of peptides help them achieve tight and specific binding to the target proteins. Increasing efforts have been made to target epigenetic readers using peptide-based inhibitors that can complement small molecules. In this review, we discuss the recent advances in the development of peptide-based inhibitors of lysine acetylation and methylation readers. |
| Persistent Identifier | http://hdl.handle.net/10722/331697 |
| ISSN | 2023 Impact Factor: 6.9 2023 SCImago Journal Rankings: 2.328 |
| ISI Accession Number ID |
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Liu, Sha | - |
| dc.contributor.author | Li, Xiang | - |
| dc.contributor.author | Li, Xin | - |
| dc.contributor.author | Li, Xiang David | - |
| dc.date.accessioned | 2023-09-21T06:58:06Z | - |
| dc.date.available | 2023-09-21T06:58:06Z | - |
| dc.date.issued | 2023-05-30 | - |
| dc.identifier.citation | Current Opinion in Chemical Biology, 2023, v. 75 | - |
| dc.identifier.issn | 1367-5931 | - |
| dc.identifier.uri | http://hdl.handle.net/10722/331697 | - |
| dc.description.abstract | <p>Inhibitors for <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/epigenetics" title="Learn more about epigenetic from ScienceDirect's AI-generated Topic Pages">epigenetic</a> readers of <a href="https://www.sciencedirect.com/topics/chemistry/histone" title="Learn more about histone from ScienceDirect's AI-generated Topic Pages">histone</a> modifications are useful chemical probes to interrogate the functional roles played by their cognate targets in <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/epigenetics" title="Learn more about epigenetic from ScienceDirect's AI-generated Topic Pages">epigenetic</a> regulation and can even serve as drugs for the treatment of diseases associated with the dysregulated targets. However, many epigenetic readers are intractable to <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/small-molecule" title="Learn more about small molecules from ScienceDirect's AI-generated Topic Pages">small molecules</a>, as the recognition of modified <a href="https://www.sciencedirect.com/topics/chemistry/histone" title="Learn more about histone from ScienceDirect's AI-generated Topic Pages">histone</a> peptides commonly involves flat and extended <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/cell-surface-protein" title="Learn more about protein surfaces from ScienceDirect's AI-generated Topic Pages">protein surfaces</a>. In contrast, the relatively large sizes and structural complexity of peptides help them achieve tight and specific binding to the target proteins. Increasing efforts have been made to target epigenetic readers using peptide-based inhibitors that can complement <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/small-molecule" title="Learn more about small molecules from ScienceDirect's AI-generated Topic Pages">small molecules</a>. In this review, we discuss the recent advances in the development of peptide-based inhibitors of lysine <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/acetylation" title="Learn more about acetylation from ScienceDirect's AI-generated Topic Pages">acetylation</a> and <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/methylation" title="Learn more about methylation from ScienceDirect's AI-generated Topic Pages">methylation</a> readers.</p> | - |
| dc.language | eng | - |
| dc.publisher | Elsevier | - |
| dc.relation.ispartof | Current Opinion in Chemical Biology | - |
| dc.subject | Chemical probe | - |
| dc.subject | Epigenetic reader | - |
| dc.subject | Lysine acetylation | - |
| dc.subject | Lysine methylation | - |
| dc.subject | Peptide-based inhibitor | - |
| dc.title | Recent advances in the development of peptide-based inhibitors targeting epigenetic readers of histone lysine acetylation and methylation marks | - |
| dc.type | Article | - |
| dc.identifier.doi | 10.1016/j.cbpa.2023.102334 | - |
| dc.identifier.scopus | eid_2-s2.0-85160529067 | - |
| dc.identifier.volume | 75 | - |
| dc.identifier.isi | WOS:001013660000001 | - |
| dc.identifier.issnl | 1367-5931 | - |