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. Docking studies show that it has a strong binding affinity with EGFR kinase, indicating its potential as a promising candidate for targeted lung cancer therapy.

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.