182249-69-0

Upstream product

• 17990-42-0 Oleanonsaeure 
• 508-02-1 Oleanolic acid 
• 1255647-21-2 C₃₇H₅₂O₄ 
• 869788-74-9 (4aS,6aS,6bR,12aR)-benzyl 2,2,6a,6b,9,9,12a-heptamethyl-10-oxo-1,2,3,4,4a,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-icosahydropicene-4a-carboxylate 

Relevant academic research and scientific papers

Synthesis and biological evaluation of oleanolic acid derivatives as inhibitors of protein tyrosine phosphatase 1B

Protein tyrosine phosphatase 1B (PTP1B) is a negative regulator in the process of insulin signaling and a promising drug target for diabetes and obesity. Derivatives of oleanolic acid were synthesized and evaluated as PTP1B inhibitors. Several derivatives exhibited moderate to good inhibitory activities against PTP1B, with 25f displaying the most promising inhibition (IC 50 = 3.12 μM). Structure-activity relationship analyses of these derivatives demonstrated that the integrity of the A ring and 12-ene moieties was important in the retention of PTP1B enzyme inhibitory activities. In addition, hydrophilic and acidic groups as well as the distance between the oleanene and acid moieties were associated with PTP1B inhibitory activities. Possible binding modes of 25f were explored by molecular docking simulations.

Ring-A cleavage of 3-oxo-olean-12-en-28-oic acid by the fungus Chaetomium longirostre

3-Oxo-olean-12-en-28-oic acid was transformed by the filamentous fungus Chaetomium longirostre into 3,4-seco-olean-12-en-4-ol-3,28-dioic acid and the 21β-hydroxylated compound. A cell-free preparation derived from the fungus converted 3-oxo-olean 12-en-28-oic acid into 3,4-seco-olean-12-en-4-ol-3,28- dioic acid. The ring-A cleavage activity was detected in the soluble fraction of the cell-free preparation and showed a requirement for NADPH.