Journal
CHEMICAL COMMUNICATIONS
Volume 58, Issue 87, Pages 12196-12199Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc04294k
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Funding
- ERC Starting Grant [715691]
- European Research Council (ERC) [715691] Funding Source: European Research Council (ERC)
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The development of stapled histone peptides bearing trimethyllysine as ligands for epigenetic reader proteins has shown stronger or weaker binding affinities compared to linear histones, indicating that selectivity towards reader proteins can be achieved.
The flexible N-terminal histone tails are a subject of numerous posttranslational modifications, including methylation. We report development of stapled histone peptides bearing trimethyllysine as ligands for epigenetic reader proteins. Stronger or weaker binding affinities have been observed for stapled histone peptides relative to linear histones, indicating that selectivity towards reader proteins can be achieved.
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