Insights into soluble guanylyl cyclase activation derived from improved heme-mimetics

Margarete Von Wantoch Rekowski, Vijay Kumar, Zongmin Zhou, Johann Moschner, Antonia Marazioti, Marina Bantzi, Georgios A. Spyroulias, Focco Van Den Akker, Athanassios Giannis, Andreas Papapetropoulos

Research output: Contribution to journalArticle

7 Scopus citations


Recently, the structure of BAY 58-2667 bound to the Nostoc sp. H-NOX domain was published. On the basis of this structural information, we designed BAY 58-2667 derivatives and tested their effects on soluble guanylyl cyclase (sGC) activity. Derivative 20 activated sGC 4.8-fold more than BAY 58-2667. Co-crystallization of 20 with the Ns H-NOX domain revealed that the increased conformational distortion at the C-terminal region of αF helix containing 110-114 residues contributes to the higher activation triggered by 20.

Original languageEnglish (US)
Pages (from-to)8948-8952
Number of pages5
JournalJournal of Medicinal Chemistry
Issue number21
StatePublished - Nov 14 2013
Externally publishedYes


ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

Cite this

Von Wantoch Rekowski, M., Kumar, V., Zhou, Z., Moschner, J., Marazioti, A., Bantzi, M., Spyroulias, G. A., Van Den Akker, F., Giannis, A., & Papapetropoulos, A. (2013). Insights into soluble guanylyl cyclase activation derived from improved heme-mimetics. Journal of Medicinal Chemistry, 56(21), 8948-8952.