pp 1-32 | Cite as

Chemical Compounds Targeting DNA Methylation and Hydroxymethylation

  • Roman Belle
  • Akane KawamuraEmail author
  • Paola B. ArimondoEmail author
Part of the Topics in Medicinal Chemistry book series


DNA methylation and its oxidised forms participate in the interpretation and regulation of the human genome. Many questions arise around the enzymes responsible for these chemical modifications on DNA, and their roles in transcriptional regulation. These epigenetic marks are very dynamic and specific in their location and context (tissues, diseases, etc.). We review the major enzymes involved in DNA methylation and oxidation, with a focus on the DNA methyltransferases and TET enzymes. The principal compounds that inhibit these enzymes are presented since they will help address these questions.


DNA hydroxymethylation DNA methylation DNMT Inhibitors TET 























5-Modified cytosine




Acute myeloid leukaemia


Active modification-passive dilution

BAH1 and BAH2

Bromo-adjacent homology domains 1 and 2


Base excision repair


CpG-binding protein, CXXC finger protein 1


Chronic myelomonocytic leukaemia


Cytidine pairing adenosine


Cytidine pairing cytidine


Cytidine pairing guanosine


Cytidine pairing thymidine


CXXC domain

DMAP domain

DNA methyltransferase-associated protein 1-interacting domain


C5-DNA methyltransferase


Double-stranded β-ηelix


Epigallocatechin gallate


Enzyme-linked immunosorbent assay


European Medicines Agency


Food and Drug Administration


Fumarate hydratase


Fat mass and obesity-associated protein


Histone deacetylase


Inhibition of the Dvl and Axin complex


Isocitrate dehydrogenase


Low-complexity insert


Liquid chromatography-mass spectrometry


Matrix-assisted laser desorption/ionisation time-of-flight


Methyl-binding protein


Myelodysplastic syndrome


Mixed lineage leukaemia


Murine TET


Naegleria gruberi TET


Nuclear localisation signal




PCNA-binding domain


Plant homeodomain


Protein arginine methyltransferase


Proline-tryptophan-tryptophan-proline domain




Replication foci targeting sequence (RFTS) domain


Repressor of silencing 1






Succinate dehydrogenase


Surface plasmon resonance


Tricarboxylic acid


Thymidine-DNA glycosylase


Ten-eleven translocation


Thin-layer chromatography


tRNA aspartic acid methyltransferase



RB is supported by the Engineering and Physical Science Research Council and University of Oxford. AK gratefully acknowledges the Royal Society for the Dorothy Hodgkin Fellowship and the European Research Council Starting Grant (EPITOOLS-679479) and the Cancer Research UK Oxford Centre Development Fund (C5255/A18085). We apologise for the incomplete citations of research due to space constraints.

The authors acknowledge the EU COST Action CM1406. PBA is supported by PlanCancer2014-2019 (EPIG-2014-01).

Compliance with Ethical Standards

Funding: RB is supported by the Engineering and Physical Science Research Council and University of Oxford. AK gratefully acknowledges the Royal Society for the Dorothy Hodgkin Fellowship and the European Research Council Starting Grant (EPITOOLS-679479) and the Cancer Research UK Oxford Centre. We apologise for the incomplete citations of research due to space constraints.

The authors acknowledge the EU COST Action CM1406. PBA is supported by PlanCancer 2014–2019 (EPIG-2014-01). PBA was recipient of the French Oversea Fellowship of the French Government and Churchill College Cambridge UK.

Conflict of Interest:

Roman Belle declares that he has no conflict of interest. Akane Kawamura declares that she has no conflict of interest and Paola B. Arimondo declares that she has no conflict of interest.

Ethical Approval:

This chapter does not contain any studies with human participants or animals performed by any of the authors.


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Copyright information

© Springer Nature Switzerland AG  2019

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of Oxford, Chemistry Research LaboratoryOxfordUK
  2. 2.Radcliffe Department of MedicineUniversity of Oxford, Wellcome Centre for Human GeneticsOxfordUK
  3. 3.Epigenetic Chemical BiologyInstitut Pasteur, CNRS UMR3523ParisFrance

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