Dream over life: Psychedelic terphenyl derivative induce hallucination via cannabinoid receptor 1

Fauzi, F A; Goh, Meng Shien; Johari, Syed Ahmad Tajudin Tuan; Hashim, Fatimah; Hassim, Muhamad Fairus Noor

doi:10.1088/1757-899x/440/1/012045

Cited by 1 publication

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“…Docking analysis was conducted to investigate the possibility of molecular interaction of NiL 2 complex with biologically important proteins. Previous studies have shown the importance of docking analysis for a synthetic compound such as thiosemicarbazide and terphenyl derivatives [ 30 , 31 ]. Interaction of NiL 2 complex with plasma retinol-binding protein 4 (RBP4) (PDB id: 5NU7) was investigated to understand its potency.…”

Section: Resultsmentioning

confidence: 99%

Synthesis, X-Ray Structure, Hirshfeld Surface Analysis, DFT Calculations, and Molecular Docking Studies of Nickel(II) Complex with Thiosemicarbazone Derivative

Osman

Silvarajoo

Hassim

et al. 2021

Bioinorganic Chemistry and Applications

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This article presents both experimental and computational study of a new Ni(II) complex, namely, bis{2-(2-trifluoromethylbenzylidene)hydrazine-1-carbothioamido-κ2N2, S}nickel(II) (abbreviate as NiL2). The complex was synthesized and well characterized using various spectroscopic methods. The single X-ray crystallographic study revealed a distorted square planar geometry around Ni(II) metal ion centre in which the angles deviated from ideal 90° with a maximum value of 6.57° occupied by nitrogen and sulphur donor atoms. The theoretical bond lengths and angles for the NiL2 complex were obtained by using the B3LYP level of density function theory (DFT) with LANL2DZ/6-311G (d, p) basis sets. These results showed very good agreement with the experimental X-ray values. The electrophilicity index (ω = 50.233 eV) shows that the NiL2 complex is a very strong electrophile. In addition, strong F⋯H/H⋯F interactions with 28.5% of the total Hirshfeld surface analyses in NiL2 were obtained indicating that the complex could bind with protein effectively. Furthermore, the new NiL2 complex was docked with plasma retinol-binding protein 4 (RBP4) (PDB id: 5NU7), which implied that the NiL2 complex bound to Tyrosine 133 and Aspartate 102 amino acids via N-H intermolecular hydrogen bonds.

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Section: Resultsmentioning

confidence: 99%