Crystal structure and Hirshfeld surface analysis of (E)-N-(2-styrylphenyl)benzenesulfonamide

Abstract

The crystal structure of the title compound C20H17NO2S features hydrogen-bonding and C—H...π interactions. Hirshfeld surface analysis revealed that H...H, C...H/H...C and O...H/H...O interactions make a major contribution to the crystal packing. Docking studies were carried out to determine the binding affinity and interaction profile of the title compound with EGFR kinase, a member of the ErbB family of receptor tyrosine kinases, which is crucial for processes such as cell proliferation and differentiation. The title compound shows a strong binding affinity with EGFR kinase, with the most favourable conformation having a binding energy of −8.27 kcal mol−1 and a predicted IC50 of 870.34 nM, indicating its potential as a promising candidate for targeted lung cancer therapy.

Keywords

• crystal structure
• synthesis
• benzenesulfonamide
• hydrogen bonding
• hirshfeld surface analysis
• docking
• egfr kinase