Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins

Peter Betlem; Marijn N. Maas; Jim Middelburg; Bas J. G. E. Pieters; Jasmin Mecinović

doi:10.1039/D2CC04294K

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Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins†

Peter Betlem,

^a Marijn N. Maas,

^b Jim Middelburg,^a Bas J. G. E. Pieters^a and Jasmin Mecinović

*^ab

Author affiliations

* Corresponding authors

^a Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands

^b Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark
E-mail: mecinovic@sdu.dk
Tel: +45-6550-3603

Abstract

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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Article information

DOI: https://doi.org/10.1039/D2CC04294K
Article type: Communication
Submitted: 01 Aug 2022
Accepted: 06 Oct 2022
First published: 06 Oct 2022

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Chem. Commun., 2022,58, 12196-12199

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Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins

P. Betlem, M. N. Maas, J. Middelburg, B. J. G. E. Pieters and J. Mecinović, Chem. Commun., 2022, 58, 12196 DOI: 10.1039/D2CC04294K

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Chemical Communications

Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins†

Abstract

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Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins

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