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Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.

Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.

期刊: ChemMedChem 日期: 2026-09-14 PMID: 42665555 DOI: 10.1002/cmdc.70442 浏览: 8
作者: Cruz-Cortés C, Šeflová J, Guerrero-Serna G, Jimenez-Vazquez EN, Anumonwo J, Espinoza-Fonseca LM
C, C.C., J, Š., G, G.S., EN, J.V., J, A., & LM, E.F. (2026). Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.. ChemMedChem. https://doi.org/10.1002/cmdc.70442
C CC, J Š, G GS, EN JV, J A, LM EF. Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.. ChemMedChem. 2026; doi: 10.1002/cmdc.70442
C CC, J Š, G GS, et al. Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.[J]. ChemMedChem. 2026. DOI: 10.1002/cmdc.70442.
@article{c2026,
  author = {Cruz-Cortés C and Šeflová J and Guerrero-Serna G and Jimenez-Vazquez EN and Anumonwo J and Espinoza-Fonseca LM},
  title = {Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.},
  journal = {ChemMedChem},
  year = {2026},
  doi = {10.1002/cmdc.70442},
  note = {PMID: 42665555},
}
TY  - JOUR
AU  - Cruz-Cortés C
AU  - Šeflová J
AU  - Guerrero-Serna G
AU  - Jimenez-Vazquez EN
AU  - Anumonwo J
AU  - Espinoza-Fonseca LM
TI  - Discovery of Ro 41-0960, a Non-Steroidal Inhibitor of the Na(+)/K(+)-ATPase.
T2  - ChemMedChem
PY  - 2026
DO  - 10.1002/cmdc.70442
AN  - PMID:42665555
ER  - 

摘要

The Na+/K+-ATPase (NKA) is a central regulator of cardiac ion homeostasis and a validated target for heart failure. Yet, cardiotonic steroids used in clinical practice are limited by a narrow therapeutic window and pro-arrhythmic effects. Here, we identify Ro 41-0960 as a non-steroidal inhibitor of NKA with a distinct mechanistic profile. The compound inhibits NKA activity with IC50 values of 17.9 ± 1.1 µM for purified enzyme and 10.3 ± 1.1 µM in microsomal preparations. ATP-dependent activity measurements revealed a non-monotonic response in which inhibition was most pronounced at ATP concentrations below 4 mM and diminished at the highest ATP concentrations tested. Docking and molecular dynamics simulations suggest that Ro 41-0960 can access both the cardiotonic steroid-binding pocket and the nucleotide-binding site; however, the ATP-dependence data are not consistent with a simple ATP-competitive mechanism. Furthermore, the compound shows only weak inhibition of SERCA (IC50 > 100 µM) and does not alter electrophysiological parameters in human iPSC-derived cardiomyocytes at concentrations producing near-maximal NKA inhibition, providing initial evidence of a favorable cardiac safety profile. Together, these findings identify Ro 41-0960 as an NKA inhibitor with a distinct chemical scaffold and provide a framework for the development of non-steroidal NKA modulators.

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