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https://www.selleckchem.com/products/ceftaroline-fosamil.html Ugonins are unique flavonoids with cyclohexyl motif from Helminthostachys zeylanica. Ugonins (1-6) from the target plant displayed significant inhibitions against both PTP1B (IC50s = 0.6-7.3 μM) and α-glucosidase (IC50s = 3.9-32.9 μM), which are crucial enzymes associated with diabetes. A cyclohexyl motif was proved to be the key functionality for PTP1B and α-glucosidase. For example, 1 was 26-fold effective to PTP1B and 15-fold to α-glucosidase than its mother compound, luteolin. This tendency was well elucidated with distinctive differences of binding affinities (KSV) between ugonins and mother compounds to PTP1B enzyme. Inhibitory mechanisms to PTP1B and α-glucosidase were fully characterized to be competitive, non-competitive and mixed type I according to the position of cyclohexyl functionality. In particular, the ugonin J (1) has a cyclohexyl on the B ring was estimated as a reversible, competitive and a slow binding inhibitor with parameters Kiapp = 0.1234 μM, k3 = 0.5713 μM-1 min-1, and k4 = 0.0705 min-1. In-depth molecular docking experiments disclosed the specific binding sites and residues of competitive inhibitor (1) and non-competitive inhibitor (4) to PTP1B enzymes. As well, all six ugonins (1-6) also inhibited α-glucosidase effectively, in which cyclohexyl motif was also the key functionality of inhibitions.An efficient approach has been made for the synthesis of a series of novel di α-aminophosphonates by the reaction of terephthalaldehyde with various pyrimidine/benzthiazole amines and diethyl phosphite using sulfonated graphitic carbon nitride - SA@g-C3N4 as catalyst under room temperature and solvent free conditions. Later, the different effects of these newly synthesized α-aminophosphonates as a function of concentration gradient has been scrutinized on the thermal and structural stability of stem bromelain (SBM) through combining the results of various spectroscopic techniques like UV

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