2. Academic Validation
  3. Organoruthenium Glycomimetics Exhibit High Selectivity and Nanomolar Affinity for Human Galectin-1

Organoruthenium Glycomimetics Exhibit High Selectivity and Nanomolar Affinity for Human Galectin-1

  • J Med Chem. 2026 Feb 26;69(4):4789-4809. doi: 10.1021/acs.jmedchem.5c03436.
Vojtěch Hamala 1,  Martin Kurfiřt 1 2,  Lucie Červenková Št́astná 1,  Filip Dvořák 1,  Jana Bernášková 1,  Adéla Sýkorová 1,  Jaroslav Kozák 3,  Martin Zavřel 3,  Tatiana Staroňová 4,  Peter Šebest 4,  Veronika Ostatná 4,  Jakub Červený 5 6,  Pavla Bojarová 5,  Jitka Holčáková 7,  Tomáš Hrstka 7,  Roman Hrstka 7,  Jindřich Karban 1
Affiliations

Affiliations

  • 1 Institute of Chemical Process Fundamentals of the Czech Academy of Sciences, Rozvojová 1/135, Praha 165 00, Czech Republic.
  • 2 Department of Organic Chemistry, University of Chemistry and Technology, Technická 5, Praha 166 28, Czech Republic.
  • 3 Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542, Praha 160 00, Czech Republic.
  • 4 Institute of Biophysics of the Czech Academy of Sciences, Královopolská 135, Brno 612 00, Czech Republic.
  • 5 Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Praha 142 00, Czech Republic.
  • 6 Department of Analytical Chemistry, Faculty of Science, Charles University, Hlavova 8, Prague 128 43, Czech Republic.
  • 7 Research Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Žlutý Kopec 7, Brno 656 53, Czech Republic.
PMID: 41643145 DOI: 10.1021/acs.jmedchem.5c03436
Abstract

Human Galectin-1 (hGal-1) is an abundant β-galactoside-binding animal lectin that plays an essential role in promoting the immunosuppressive tumor microenvironment. Although hGal-1 has been identified as a promising target for pharmacological inhibition, developing potent and selective hGal-1 inhibitors has been complicated by the high degree of sequence similarity of the glycan-binding site across the Galectin family. Herein, we present potent nanomolar hGal-1 inhibitors with unprecedented selectivity of 2 to 3 orders of magnitude over human Galectin-3 (hGal-3). Their primary structural feature is the modification of a thiodigalactoside scaffold at the 3- and 3'-positions with a half-sandwich ruthenium(II) arene complex containing a bidentate 4-(2-pyridyl)-1H-1,2,3-triazol-1-yl ligand. The most potent inhibitor in the series efficiently blocked the binding of hGal-1 to the surface of MDA-MB-231 tumor cells, reduced their viability, and completely suppressed hGal-1-induced phosphatidylserine exposure in Jurkat cells, a process previously described as preaparesis rather than classical Apoptosis.

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