PRMT Inhibitors

Part of the Topics in Medicinal Chemistry book series (TMC, volume 33)


The methylation of arginine residues in numerous protein targets is a post-translational modification that has gained increased interest in the scientific community over the past two decades. Arginine methylation is performed by the dedicated family of protein arginine methyltransferases and is known to be involved in a plethora of cellular pathways and biochemical mechanisms in both healthy and disease states. The development of inhibitors for these enzymes for use as biological tools can lead to a more detailed understanding of the functions of the different members of the PRMT family. In addition, a number of recent studies point towards PRMTs as therapeutic targets for a number of diseases and the first clinical trials with compounds inhibiting PRMTs are now underway. We here provide a broad overview of the current status of the inhibitors that have been developed against PRMTs using both high-throughput screening and rational design approaches.


Activity Inhibition Methylation Protein arginine N-methyltransferase Therapeutics 



Asymmetrically dimethylated arginine






Adenosine dialdehyde


Arginine methyltransferase inhibitor


Acute myeloid leukaemia


Coactivator-associated arginine methyltransferase


Deoxyribonucleic acid


Epstein-Barr virus


Half maximal effective concentration


Glycine-arginine rich


Human embryonic kidney cell line


Hepatocellular carcinoma cell line


Human immunodeficiency virus


Half maximal inhibitory concentration


Inhibition constant


Lymph node carcinoma of the prostate, prostate cancer cell line


Michigan Cancer Foundation-7, breast cancer cell line


Mantle cell lymphoma


Methylosome protein 50


Mixed lineage leukaemia


Monomethylated arginine




5-Methylthioadenosine phosphorylase


Poly(A)-binding protein-1


Protein arginine deiminase


Proline, glycine, methionine-rich




Protein arginine N-methyltransferase


Ribonucleic acid


Repressor splicing factor




S-adenosyl-l-homocysteine hydrolase




Structure-activity relationship


Symmetrically dimethylated arginine


SET domain containing protein 7


Structural genomics consortium


Trans-activator of transcription


Compliance with Ethical Standards

Funding: The support of Leiden University is kindly acknowledged.

Conflict of Interest: Matthijs van Haren declares that he has no conflict of interest. Nathaniel I. Martin declares that he has no conflict of interest.

Ethical Approval: This article does not contain any studies with human participants or animals performed by any of the authors.


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© Springer Nature Switzerland AG  2019

Authors and Affiliations

  1. 1.Biological Chemistry Group, Institute of Biology LeidenLeiden UniversityLeidenThe Netherlands

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