Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 22nd May 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.

Issue 2, 2017
Previous Article Next Article

Discovery of decamidine as a new and potent PRMT1 inhibitor

Author affiliations


Protein arginine methyltransferase 1 (PRMT1) is a key player for the dynamic regulation of arginine methylation. Its dysregulation and aberrant expression are implicated in various pathological conditions, and a plethora of evidence suggests that PRMT1 inhibition is of significant therapeutic value. Herein, we reported the modification of a series of diamidine compounds with varied lengths in the middle alkyl linker for PRMT1 inhibition. Decamidine (2j), which possesses the longest linker in the series, displayed 2- and 4-fold increase in PRMT1 inhibition (IC50 = 13 μM), compared with furamidine and stilbamidine. The inhibitory activity toward PRMT1 was validated by secondary orthogonal assays. Docking studies showed that the increased activity is due to the extra interaction of the amidine group with the SAM binding pocket, which is absent when the linker is not long enough. These results provide structural insights into developing the amidine type of PRMT1 inhibitors.

Graphical abstract: Discovery of decamidine as a new and potent PRMT1 inhibitor

Back to tab navigation

Supplementary files

Publication details

The article was received on 13 Oct 2016, accepted on 30 Dec 2016 and first published on 03 Jan 2017

Article type: Research Article
DOI: 10.1039/C6MD00573J
Med. Chem. Commun., 2017,8, 440-444

  •   Request permissions

    Discovery of decamidine as a new and potent PRMT1 inhibitor

    J. Zhang, K. Qian, C. Yan, M. He, B. A. Jassim, I. Ivanov and Y. G. Zheng, Med. Chem. Commun., 2017, 8, 440
    DOI: 10.1039/C6MD00573J

Search articles by author