Structures, Photoresponse Properties, and Biological Activity of Dicyano-Substituted 4-Aryl-2-pyridone Derivatives

Abstract

Described in this work is the synthesis of a novel dicyano-substituted N -2-aminoethyl-4-(3-pyridinyl)-2-pyridone organic compound ( 1 ) that is characterized by several spectroscopic methods. Compound ( 1 ) was utilized for the preparation of its perchlorate ( 2 ), chloride ( 3 ), and bromide ( 4 ) salts. Single-crystal X-ray structures of these three salts were determined, and noncovalent weak interactions involving the aromatic rings, anions, and water molecules in ( 2 – 4 ) were investigated in detail. Solid-state UV–vis spectrum of the reported compounds ( 1 – 4 ) was utilized to calculate their optical band gaps, which clearly indicated that they belong to the semiconductor family. Under illumination condition, the magnitudes of electrical properties of ( 1 ) and its salts ( 2 – 4 ) improve remarkably although the improvement differs from salt to salt and the result was analyzed theoretically. Salt ( 2 ) was tested for its DNA binding ability.

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Insight into charge transportation in cadmium based semiconducting organic–inorganic hybrid materials and their application in the fabrication of photosensitive Schottky devices

“…15). [55][56][57][58][59][60] To calculate the optical response and taking into consideration the calculated band structure (Fig. 13), we have chosen a photon-energy range of 0-10 eV.…”

Experimental and theoretical studies of 1,3,5‐tris (bromomethyl)‐2,4,6‐trimethylbenzene with 2‐pyridone

“…It was observed that the compound can bind to the DNA helix in a partial intercalative manner. [26] Density functional theory (DFT) calculations in conjugation with molecular docking analysis are inevitable in exposing the nature of interactions between compounds and protein in recent years. [27,28] It is important to note that various forces including hydrogen bonding, π-π stacking, and electrostatic interactions along with other non-covalent interactions help the molecules to be intact inside the binding pocket of proteins.…”