Synthesis, SCXRD, Hirshfeld analysis, DFT, molecular docking, in vitro anti-cancer, anti-diabetic and anti-inflammatory activities of (E)-4-[(4-hydroxybenzylidene)hydrazinyl]benzonitrile

•Single crystals of (E)−4-(2-(4-hydroxybenzylidene)hydrazinyl)benzonitrile (HHBN) have been synthesized using slow evaporation method.•The different functional groups and crystal structure were characterized using single-crystal XRD, UV–Vis spectroscopy, fourier transform infrared (FT-IR), proton (1H), and carbon (13C) nuclear magnetic resonance (NMR) spectroscopy.•Quantum mechanical calculations were performed using the B3LYP/6–311++G(d,p) method in GAUSSIAN 09 software to determine the optimized geometry, vibrational assignments, natural bond orbitals (NBO) and frontier molecular orbitals (FMO).•To evaluate enzyme inhibitory activity, molecular docking interactions were performed against the homology model of prostaglandin H2 syntheses cyclooxygenase (1PGG.pdb) and the human pancreatic amylase enzyme (1HNY.pdb).•To evaluate biological in vitro applications, the anti-cancer, anti-inflammatory and anti-diabetic properties were investigated. (E)-4-[(4-hydroxybenzylidene)hydrazinyl]benzonitrile (HHBN) has been synthesized and defect free single crystals were grown by slow evaporation technique using ethanol as solvent. The single crystal XRD measurement of HHBN belongs to a monoclinic system with unit space group P21/c. The unit cell characteristics are a = 5.8573(7), b = 7.3927(10), c = 27.7190(3), V = 1196.1(3) (Å3), and Z = 4. Notably, the crystal structure of HHBN is stabilized by intermolecular C–H···O and O–H···N interactions. The voids energy frame works and interaction energy between molecules also studied using Hirshfeld surfaces. The distribution of electron density and the interaction between orbitals can be examined through natural bond orbital analysis, providing insights into the compound's stability and reactivity. Biological in vitro studies such as anti-cancer, anti-diabetic and anti-inflammatory evaluations were carried out. To demonstrate enzyme inhibitory activity, molecular docking interactions were performed against the homology model of prostaglandin H2 synthase cyclooxygenase (1PGG), human pancreatic-amylase enzyme (1HNY) and epidermal growth factor receptors (5HG7). The title molecule exhibited very strong binding energiesand demonstrated three distinct hydrogen bonding interactions with the amino acid residues of the 1HNY, 1PGG and 5HG7 enzymes. [Display omitted]