This study demonstrates that replacing a planar phenyl group with a 3D ortho-carborane cage in a peptidomimetic inhibitor significantly enhances binding to the parasitic protease SmCB1 and improves anti-schistosomal activity. Structural and quantum-mechanical analyses reveal that this improvement arises from a unique CH-based hydrogen bond and strong electrostatic interactions driven by the large dipole moment of the carborane cage. The work highlights carborane moiety within the inhibitor as a powerful pharmacophore capable of boosting ligand affinity in protein environments with specific steric and electrostatic features.
More information in the article: https://pubs.rsc.org/en/content/articlelanding/2026/qi/d5qi01546d
And a delightful piece of news to conclude: this article is featured on the cover of the journal. Warm congratulations to all the authors!
