**Background**
Poly(ADP-ribose) polymerases (PARPs) are a family of enzymes involved in critical cellular processes, including DNA repair, genomic stability, and the regulation of programmed cell death. Among these, PARP-1 (ARTD-1) plays a central role in detecting DNA single-strand breaks and coordinating the cellular response to genomic damage. Due to its essential role in maintaining DNA integrity, PARP-1 has become a primary target for the development of therapeutic agents, particularly in the field of oncology. Inhibition of PARP-1 can lead to the accumulation of DNA lesions, triggering synthetic lethality in cells with deficient DNA repair mechanisms. In this context, we will introduce a potent and selective PARP-1 inhibitor – EB-47.
**Definition**
EB-47 is a potent and selective PARP-1/ARTD-1 inhibitor with an IC50 value of 45 nM. According to the EB-47 description, this compound mimics the substrate NAD+ and extends from the nicotinamide to the adenosine subsite.
**In Vitro and In Vivo Studies**
The EB-47 biological activity has been evaluated across various targets and models. In vitro studies demonstrate that EB-47 dihydrochloride shows inhibition in excess of 50% with CdPARP. Specifically, it is capable of inhibiting CdPARP and HsPARP with IC50 values of 0.86 and 1.0 μM, respectively. Furthermore, EB-47 exhibits modest potency against ARTD5, with an IC50 value of 410 nM. Regarding the EB-47 In Vivo application, research indicates that the administration of EB-47 dihydrochloride (2 μM; 5 days) decreases the number of blastocysts and embryo implantation sites at day 5, highlighting the role of PARP1 in the process of embryo implantation. For researchers requiring specific EB-47 technical information, the compound is characterized by a molecular weight of 610.45 and the chemical formula C24H29Cl2N9O6. In conclusion, EB-47 is a potent and selective inhibitor of PARP-1 with significant potential for research into DNA repair and reproductive biology.
Keywords
EB-47, 1190332-25-2, EB47, EB 47, PARP, poly ADP ribose polymerase, PARP-1, ARTD-1, cardiac, reperfusion, NAD, cerebral, arterial, occlusion, ARTD5
References
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[2] García-Saura AG, et al. Comparative inhibitory profile and distribution of bacterial PARPs, using Clostridioides difficile CD160 PARP as a model. Sci Rep. 2018 May 23;8(1):8056.
[3] Jagtap PG, et al. The discovery and synthesis of novel adenosine substituted 2,3-dihydro-1H-isoindol-1-ones: potent inhibitors of poly(ADP-ribose) polymerase-1 (PARP-1).Bioorg Med Chem Lett. 2004 Jan 5;14(1):81-5.