An ecofriendly, magnetically retrievable amine-functionalized SiO2@Fe3O4 catalyst was successfully synthesized and affirmed by several physicochemical characterization tools, such as scanning electron microscopy (SEM), transmission electron microscopy (TEM), Fourier-transform infrared spectroscopy (FT-IR), vibrating sample magnetometry (VSM), energy-dispersive X-ray spectroscopy (EDX), and powder X-ray diffraction. Thereafter, the catalytic performance of this environmentally benign NH2@SiO2@Fe3O4 catalyst was investigated in the one-pot multicomponent synthesis of 2-amino-4H-benzo­[b]­pyran derivatives. The reaction was simply achieved by grinding of various substituted aromatic aldehydes, dimedone, and malononitrile at room temperature under solvent and waste-free conditions with excellent yields and high purity. Moreover, the developed catalyst not only possesses immense potential to accelerate the synthesis of bioactive pyran derivatives but also exhibits several remarkable attributes like broad functional group tolerance, durability, improved yield, reusability, and recyclability. Besides, various other fascinating advantages of this protocol are milder reaction conditions, cost effectiveness, short reaction time, and simple work up procedures.

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Dispiro-tetraoxanes, a class of fully synthetic peroxides which can be used as an antiplasmodial remedy for multiple drug-resistant strains of Plasmodium falciparum, were selected for the interaction study with human serum albumin (HSA). The insight into the interaction of the two chemically synthesized, most potent antimalarial tetraoxane analogues (TO1 and TO2) and HSA has been scrutinized using distinct spectroscopic techniques such as. UV–visible absorption, fluorescence, time-resolved fluorescence, and circular dichroism (CD). Fluorescence quenching experiments divulged the static mode of quenching and binding constants obtained (∼104) indicated the moderate affinity of the analogues to HSA. CD confirmed the conformational changes in the serum albumin upon interaction with these analogues. Molecular docking validated the empirical results as these two analogues bind through hydrophobic interactions and hydrogen bonding with HSA. Present work first defined the binding mechanism of dispiro-tetraoxanes with HSA and thus provides a fresh insight into the drug transportation and metabolism. The present study could direct toward designing more potent tetraoxane analogues for their use in the biomedical field.