The development and characterization of a chemical probe targeting PRMT1 over PRMT5

Authors

Sarah A. Mann, University of North Florida
Andrew Salsburg, University of North Florida
Corey P. Causey, University of North FloridaFollow
Bryan Knuckley, University of North FloridaFollow

Document Type

Article

Publication Date

1-1-2019

Abstract

Protein arginine methyltransferases (PRMTs) are a family of mammalian enzymes catalyzing the symmetric dimethylation (Type I), asymmetric dimethylation (Type II), or monomethylation (Type III) of arginine residues within proteins. This family is composed of 11 isozymes, however the vast majority of asymmetric and symmetric dimethylation in mammals is completed by either PRMT1 or PRMT5, respectively. In recent years, a number of chemical probes targeting this family of enzymes have been developed, but the majority of these probes lack isozyme specificity. Herein, we report the development of a chemical probe, based on a non-natural peptide sequence, which specifically labels PRMT1 over PRMT5 with high selectivity and sensitivity.

Publication Title

Bioorganic and Medicinal Chemistry

Volume

27

Issue

1

First Page

224

Last Page

229

Digital Object Identifier (DOI)

10.1016/j.bmc.2018.12.001

PubMed ID

30529151

ISSN

09680896

E-ISSN

14643391

Citation Information

Mann, Sarah A.; Salsburg, Andrew; Causey, Corey P.; and Knuckley, Bryan, "The development and characterization of a chemical probe targeting PRMT1 over PRMT5" (2019). UNF Faculty Research and Scholarship. 1013.
https://digitalcommons.unf.edu/unf_faculty_publications/1013