16554-53-3Relevant articles and documents
Supramolecular Interaction of Molecular Cage and β-Galactosidase: Application in Enzymatic Inhibition, Drug Delivery and Antimicrobial Activity
Mondal, Avijit,Bhat, Imtiyaz Ahmad,Karunakaran, Subbaraj,De, Mrinmoy
, p. 1955 - 1960 (2021)
Enzyme inhibitors play a crucial role in diagnosis of a wide spectrum of diseases related to bacterial infections. We report here the effect of a water-soluble self-assembled PdII8 molecular cage towards β-galactosidase enzyme activity. The molecular cage is composed of a tetrapyridyl donor (L) and cis-[(en)Pd(NO3)2] (en=ethane-1,2-diamine) acceptor and it has a hydrophobic internal cavity. We have observed that the acceptor moiety mainly possesses the ability to inactivate the β-galactosidase enzyme activity. Kinetic investigation revealed the mixed mode of inhibition. This inhibition strategy was extended to control the growth of methicillin-resistant Staphylococcus aureus. The internalization of the Pd(II) cage inside the bacteria was confirmed when bacterial solutions were incubated with curcumin loaded cage. The intrinsic green fluorescence of curcumin made the bacteria glow when put under an optical microscope. Furthermore, this curcumin loaded molecular cage shows an enhanced antibacterial activity. Thus, PdII8 molecular cage is quite attractive due to its dual role as enzyme inhibitor and drug carrier.
High catalytic efficiency of nanostructured β-CoMoO4 in the reduction of the ortho-, meta- and para-nitrophenol isomers
Al-Wadaani, Fahd,Omer, Ahmed,Abboudi, Mostafa,Hassani, Hicham Oudghiri,Rakass, Souad,Messali, Mouslim,Benaissa, Mohammed
, (2018/02/17)
Nanostructured -CoMoO4 catalysts have been prepared via the thermal decomposition of an oxalate precursor. The catalyst was characterized by infrared spectroscopy (FTIR), X-ray diffraction (XRD), Brunauer-Emmett-Teller method (BET), energy dispersive X-ray spectroscopy (EDX), and transmission electron microscopy (TEM). The efficiency of these nanoparticles in the reduction of ortho- and meta-nitrophenol isomers (2-NP, 3-NP, and 4-NP) to their corresponding aminophenols was tested using UV-visible spectroscopy measurements. It was found that, with a -CoMoO4 catalyst, NaBH4 reduces 3-NP instantaneously, whilst the reduction of 2-NP and 4-NP is slower at 8 min. This difference is thought to arise from the lower acidity of 3-NP, where the negative charge of the phenolate could not be delocalized onto the oxygen atoms of the meta-nitro group.
Evaluating binuclear copper(II) complexes for glycoside hydrolysis
Striegler, Susanne,Dunaway, Natasha A.,Gichinga, Moses G.,Barnett, James D.,Nelson, Anna-Gay D.
experimental part, p. 2639 - 2648 (2010/06/20)
Three binuclear copper(II) complexes were characterized as solids by X-ray diffraction and in solution by UV/vis spectrophotometric titration, and subsequently evaluated for their glycosidase-like activity. The structure analysis revealed comparable intermetallic Cu ? ? ? Cu distances (~3.5 A) for the complexes 2 and 3. Despite this similarity, the composition of the complexes differs significantly in aqueous solution as revealed by spectrophotometric titrations. The hydrolysis of selected nitrophenylglycopyranosides is up to 11,000-fold accelerated over background in the presence of the copper(II) complexes in 3-(cyclohexylamino)-1- propanesulfonic acid (CAPS) buffer at pH 10.5 and 30 °C.
