Neighboring-group participation by C-2 ether functions in glycosylations directed by nitrile solvents

Ether-protecting functions at C-2 hydroxy groups have been found to play participating roles in glycosylations when the reactions are conducted in nitrile solvent mixtures. The participation mechanism is based on intramolecular interaction between the lone electron pair of the oxygen atom of the C-2 ether function and the nitrile molecule when they are positioned in a cis configuration. A 1,2-cis glycosyl oxazolinium intermediate is formed. This participation, in conjunction with the anomeric effect of the glycosyl donor, confers high 1,2-trans selectivities on glycosylations. Further application of this concept has led to efficient preparations of α-(1→5)-arabinan oligomers.     

Chromogenic spray reagent for the detection and identification of amitraz in biological materials

JPC – Journal of Planar Chromatography – Modern TLC - In the present study, we developed a simple, sensitive, and selective thin-layer chromatographic method for the detection and...     

Microwave Promoted,Sodium Acetate Catalyzed One Pot Synthesis of Poly Functionalized 4H‐Pyrans

A clean and efficient one pot synthesis of 4H‐pyran derivatives through condensation of aromatic aldehydes, malononitrile and dicarbonyl compounds under microwave irradiation in presence of Sodium acetate as a catalyst is described.     

Fluorescent probes of tissue transglutaminase reveal its association with arterial stiffening

Tissue transglutaminase (TG2) catalyzes the crosslinking of proteins. TG2 has been implicated in fibrosis and vascular calcification, both of which lead to a common feature of aging known as arterial stiffness. In order to probe the role of TG2 in arterial rigidification, we have prepared a fluorescent irreversible inhibitor as a probe for TG2 activity (RhodB-PGG-K(Acr)-LPF-OH). This probe was synthesized on solid support, characterized kinetically (k(inact) = 0.68 min?1, K(I) = 79 μM), and then used to stain the aorta from rats used as a model of isolated systolic hypertension (ISH). Interestingly, TG2 activity was thus shown to increase over 4 weeks of the hypertension model, corresponding with the previously observed increase in arterial stiffness. These results clearly suggest an association between TG2 and the phenomenon of arterial rigidification.     

PEG-SO3H: A mild and efficient recyclable catalyst for the synthesis of coumarin derivatives

A simple and efficient synthesis of coumarin derivatives through condensation reaction of substituted phenols and dicarbonyl compounds using PEG-SO₃H as a recyclable catalyst under solvent-free conditions is described.     

Detection of amitraz,a formamidine-based pesticide using chromogenic spray reagent by thin-layer chromatography

JPC – Journal of Planar Chromatography – Modern TLC - In the present study, we developed a simple, sensitive and selective thin-layer chromatographic method for the detection and...     

Site-specific protein propargylation using tissue transglutaminase

Transglutaminases (TGases) catalyse the transamidation of glutamine residues with primary amines. Herein we report the first FRET-based activity assay for the direct detection of the ligation (transamidation) reaction mediated by tissue TGase (TG2). This novel assay was then used in a microtiter plate-based screen of a library of 18 potential amine substrates. From this screen it was discovered that propargyl amine serves as an excellent substrate for TG2. Subsequently, propargyl amine and 2-azidoethyl amine were validated independently as TG2 substrates with K(M) values of 44 ± 4 μM, and 0.99 ± 0.06 mM, respectively. In a proof-of-principle protein labelling experiment, the protein casein was selectively functionalized with propargyl amine using TG2 and subsequently fluorescently labelled through a dipolar cycloaddition reaction with an azido-fluorescein conjugate. This application demonstrates the strong potential of using TG2 for site-specific protein modification through a combination of enzymatic and bioorthogonal chemistry.