588-07-8Relevant articles and documents
One-Pot Regioselective and Stereoselective Synthesis of C-Glycosyl Amides from Glycals Using Vinyl Azides as Glycosyl Acceptors
Rasool, Faheem,Ahmed, Ajaz,Hussain, Nazar,Yousuf, Syed Khalid,Mukherjee, Debaraj
, p. 4036 - 4039 (2018)
The reaction of glycals containing good leaving groups with aromatic vinyl azides to give α-C-glycosyl amides in good yields is described. Various vinyl azides with different groups undergo the reaction smoothly. In these reactions, an iminodiazonium intermediate is generated by the attack of the vinyl azide onto the glycal under Lewis acid conditions. This undergoes Schmidt-type denitrogenative 1,2-migration to form a nitrilium ion, which, upon hydrolysis, gives the desired C-glycosyl amide.
Hydrosilylative reduction of primary amides to primary amines catalyzed by a terminal [Ni-OH] complex
Bera, Jitendra K.,Pandey, Pragati
supporting information, p. 9204 - 9207 (2021/09/20)
A terminal [Ni-OH] complex1, supported by triflamide-functionalized NHC ligands, catalyzes the hydrosilylative reduction of a range of primary amides into primary amines in good to excellent yields under base-free conditions with key functional group tolerance. Catalyst1is also effective for the reduction of a variety of tertiary and secondary amides. In contrast to literature reports, the reactivity of1towards amide reduction follows an inverse trend,i.e., 1° amide > 3° amide > 2° amide. The reaction does not follow a usual dehydration pathway.
Design, synthesis, kinetic, molecular dynamics, and hypoglycemic effect characterization of new and potential selective benzimidazole derivatives as Protein Tyrosine Phosphatase 1B inhibitors
Campos-Almazán, Mara Ibeth,Flores-Ramos, Miguel,Hernández-Campos, Alicia,Castillo, Rafael,Sierra-Campos, Erick,Torgeson, Kristiane,Peti, Wolfgang,Valdez-Solana, Mónica,Oria-Hernández, Jesús,Méndez, Sara T.,Castillo-Villanueva, Adriana,Jiménez-de Jesús, Hugo,Avitia-Domínguez, Claudia,Téllez-Valencia, Alfredo
, (2021/09/28)
Protein-tyrosine phosphatase 1B (PTP1B) is a negative regulator of insulin signaling pathway and has been validated as a therapeutic target for type 2 diabetes. A wide variety of scaffolds have been included in the structure of PTP1B inhibitors, one of them is the benzimidazole nucleus. Here, we report the design and synthesis of a new series of di- and tri- substituted benzimidazole derivatives including their kinetic and structural characterization as PTP1B inhibitors and hypoglycemic activity. Results show that compounds 43, 44, 45, and 46 are complete mixed type inhibitors with a Ki of 12.6 μM for the most potent (46). SAR type analysis indicates that a chloro substituent at position 6(5), a β-naphthyloxy at position 5(6), and a p-benzoic acid attached to the linker 2-thioacetamido at position 2 of the benzimidazole nucleus, was the best combination for PTP1B inhibition and hypoglycemic activity. In addition, molecular dynamics studies suggest that these compounds could be potential selective inhibitors from other PTPs such as its closest homologous TCPTP, SHP-1, SHP-2 and CDC25B. Therefore, the compounds reported here are good hits that provide structural, kinetic, and biological information that can be used to develop novel and selective PTP1B inhibitors based on benzimidazole scaffold.