Akademik Veri Yönetim Sistemi
JOURNAL OF COMPUTATIONAL BIOPHYSICS AND CHEMISTRY, 2026 (SCI-Expanded, Scopus)
This investigation focuses on the design, synthesis, comprehensive analysis and binding affinity with the epidermal growth factor receptor (EGFR), Cyclin-Dependent Kinase 6 (CDK6) of a new 1,8-naphthyridine-pivalamide hybrid 1. The newly synthesized 1,8-naphthyridine-pivalamide hybrid 1 was characterized by FT-IR, H-1 NMR, elemental analysis and single-crystal X-ray analysis. The crystal structure analysis disclosed that 1 is hydrated and supramolecular assembly is stabilized via O-H & ctdot;N, N-H & ctdot;O, and O-H & ctdot;O and off-set pi & ctdot;pi contacts. Various types of noncovalent contacts existing in the 1,8-naphthyridine-pivalamide hybrid 1 are explored, and subsequently quantified employing Hirshfeld surface analysis and 2D fingerprint plots. Furthermore, a void study was utilized to examine the mechanical stability and presence of the cavity within the solid-state structure of 1. The interaction energies between molecules in 1 have been investigated using the interaction energy calculation. Geometric parameters of the optimized structure of 1 were determined utilizing the DFT calculations. Furthermore, molecular docking studies indicated that the 1,8-naphthyridine-pivalamide hybrid 1 demonstrated promising binding affinity with EGFR and CDK6, compared to their known inhibitors. The newly synthesized 1,8-naphthyridine-pivalamide hybrid 1 also exhibited drug-likeness as predicted by SwissADME.