This review focuses on the application of vinyl azide in organic synthesis and highlights new strategies and methods using this compound to produce heterocycles and other organic compounds.

The stilbenes are undoubtedly one of the most significant moieties in various bioactive natural and synthetic structures, and they are considered as the privileged structures. Hence, preparation of such structures...

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In this paper, a novel catalyst is introduced based on the immobilization of palladium onto magnetic Fucus Vesiculosus extract (Pd@mFuVe catalyst). For the synthesis of Pd@mFuVe catalyst, Fucus Vesiculosus extract is obtained from the plant source, followed by the synthesis of superparamagnetic iron oxide nanoparticles (SPION) onto the extract. The catalyst is characterized by several methods, including scanning electron microscopy (SEM), energy-dispersive X-ray spectroscopy (EDS), FT-IR spectroscopy, vibrating sample magnetometer (VSM), powder X-ray diffraction analysis (XRD), and inductively coupled plasma (ICP). The activity of Pd@mFuVe catalyst is studied in the synthesis of N-alkyl-2-(4-methyl-1-oxoisoquinolin-2(1H)-yl)-2-phenylacetamides. The products were synthesized in three steps, the synthesis of 2-iodobenzoic acid from 2-aminobenzoic acid, which participated in a multicomponent reaction with allylamine, aldehydes, and isocyanides, followed by a cyclization reaction, catalyzed by Pd@mFuVe catalyst. The product yields are high and the catalyst showed good reusability after 5 sequential runs. The most significant, Pd@mFuVe catalyst is fabricated from a plant extract source as a green support for the catalyst.

Herein, a straightforward synthetic strategy mediated by Ugi reaction was developed to synthesize novel series of compounds as tyrosinase inhibitors. The structures of all compounds were confirmed by FT‐IR, 1H‐NMR, 13C‐NMR, and CHNOS techniques. The tyrosinase inhibitory activities of all synthesized derivatives 5a–m were determined against mushroom tyrosinase and it was found that derivative 5c possesses the best inhibition with an IC50 value of 69.53±0.042 μM compared to the rest of the synthesized derivatives. Structure–activity relationships (SARs) showed that the presence of 4‐MeO or 4‐NO2 at the R2 position plays a key role in tyrosinase inhibitory activities. The enzyme kinetics studies showed that compound 5c is an noncompetitive inhibitor. For in silico study, the allosteric site detection was first applied to find the appropriate binding site and then molecular docking and molecular dynamic studies were performed to reveal the position and interactions of 5c as the most potent inhibitor within the tyrosinase active site. The results showed that 5c bind well with the proposed binding site and formed a stable complex with the target protein.