Hydrogenation of β-isocinchonicine in mild conditions on Pt and Pd catalysts using HPLC-ESI-ion-trap MS: New results on the role of structure of cinchona alkaloids in the Orito reaction

2006 ◽  
Vol 7 (2) ◽  
pp. 104-108 ◽  
Author(s):  
Imre Bucsi ◽  
Mária Sutyinszki ◽  
Károly Felföldi ◽  
Mihály Bartók
Author(s):  
Xiaojiao Cai ◽  
Siyuan Fang ◽  
Yun Hang Hu

Direct and highly efficient methane conversion to methanol under mild conditions is achieved via photocatalysis over Au–Pd/TiO2.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Fariba Peytam ◽  
Ghazaleh Takalloobanafshi ◽  
Toktam Saadattalab ◽  
Maryam Norouzbahari ◽  
Zahra Emamgholipour ◽  
...  

AbstractIn an attempt to find novel, potent α-glucosidase inhibitors, a library of poly-substituted 3-amino-2,4-diarylbenzo[4,5]imidazo[1,2-a]pyrimidines 3a–ag have been synthesized through heating a mixture of 2-aminobenzimidazoles 1 and α-azidochalcone 2 under the mild conditions. This efficient, facile protocol has been resulted into the desirable compounds with a wide substrate scope in good to excellent yields. Afterwards, their inhibitory activities against yeast α-glucosidase enzyme were investigated. Showing IC50 values ranging from 16.4 ± 0.36 µM to 297.0 ± 1.2 µM confirmed their excellent potency to inhibit α-glucosidase which encouraged us to perform further studies on α-glucosidase enzymes obtained from rat as a mammal source. Among various synthesized 3-amino-2,4-diarylbenzo[4,5]imidazo[1,2-a]pyrimidines, compound 3k exhibited the highest potency against both Saccharomyces cerevisiae α-glucosidase (IC50 = 16.4 ± 0.36 μM) and rat small intestine α-glucosidase (IC50 = 45.0 ± 8.2 μM). Moreover, the role of amine moiety on the observed activity was studied through substituting with chlorine and hydrogen resulted into a considerable deterioration on the inhibitory activity. Kinetic study and molecular docking study have confirmed the in-vitro results.


Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 4083
Author(s):  
Heming Jiang ◽  
Tian-Yu Sun

A computational study on the origin of the activating effect for Pd-catalyzed directed C–H activation by the concerted metalation-deprotonation (CMD) mechanism is conducted. DFT calculations indicate that strong acids can make Pd catalysts coordinate with directing groups (DGs) of the substrates more strongly and lower the C–H activation energy barrier. For the CMD mechanism, the electrophilicity of the Pd center and the basicity of the corresponding acid ligand for deprotonating the C–H bond are vital to the overall C–H activation energy barrier. Furthermore, this rule might disclose the role of some additives for C–H activation.


2010 ◽  
Vol 274 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Lequan Liu ◽  
Feng Zhou ◽  
Liguo Wang ◽  
Xiujuan Qi ◽  
Feng Shi ◽  
...  

2020 ◽  
Vol 11 (19) ◽  
pp. 5043-5051
Author(s):  
Jian Yang ◽  
Verònica Postils ◽  
Michael I. Lipschutz ◽  
Meg Fasulo ◽  
Christophe Raynaud ◽  
...  

A cationic nickel complex of the bis(8-quinolyl)(3,5-di-tert-butylphenoxy)phosphine (NPN) ligand, [(NPN)NiCl]+, is a precursor to efficient catalysts for the hydrosilation of alkenes with hydrosilanes under mild conditions and low catalyst loadings.


ACS Catalysis ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 6071-6083 ◽  
Author(s):  
Shixiang Feng ◽  
Jun Yi ◽  
Hiroki Miura ◽  
Naoki Nakatani ◽  
Masahiko Hada ◽  
...  

1968 ◽  
Vol 107 (1) ◽  
pp. 41-49 ◽  
Author(s):  
G. M. Herring

A fraction containing chondroitin sulphate, isolated from bovine cortical bone under mild conditions, was separated by ion-exchange chromatography into three fractions with apparent homogeneity on electrophoresis and ultracentrifugation. Two of these appeared to consist of chondroitin sulphate bound to a glycoprotein ‘core’ that had similarities to the bone sialoprotein described previously. The differences in composition of the two fractions were considered to be due to variation in the number or lengths of the polysaccharide chains. The presence of xylose and the alkali-lability of the bond between protein and polysaccharide suggested the presence of a xylosylserine linkage. The third fraction had the properties of a relatively pure chondroitin sulphate which contained a small amount of peptide. These fractions differed considerably from the protein–polysaccharide complexes of epiphysial and other cartilages, and their relevance to the possible role of glycosaminoglycans is discussed.


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