35485-78-0Relevant articles and documents
Design and synthesis of novel photoaffinity probes for study of the target proteins of oleanolic acid
Zhang, Liying,Zhang, Yingxia,Dong, Jizhe,Liu, Jun,Zhang, Luyong,Sun, Hongbin
, p. 1036 - 1039 (2012/03/26)
To explore the molecular mechanisms of oleanolic acid, two novel photoaffinity probes were synthesized based on the structure-activity relationship reported previously. Their potency were evaluated in an enzyme inhibition assay against rabbit muscle glycogen phosphorylase a (RMGPa), a known target protein of oleanolic acid. The inhibitory activity of probe 2 was only about two-fold less potent than the mother compound oleanolic acid. The photoaffinity labeling experiments were also performed and two proteins were specifically tagged by probe 2. The results suggest that the synthesized probes could be used as powerful tools to isolate and identify the target proteins of oleanolic acid.
Penicillin inhibitors of purple acid phosphatase
Faridoon,Hussein, Waleed M.,Ul Islam, Nazar,Guddat, Luke W.,Schenk, Gerhard,McGeary, Ross P.
supporting information; experimental part, p. 2555 - 2559 (2012/05/20)
Purple acid phosphatases (PAPs) are binuclear metallohydrolases that have a multitude of biological functions and are found in fungi, bacteria, plants and animals. In mammals, PAP activity is linked with bone resorption and over-expression can lead to bone disorders such as osteoporosis. PAP is therefore an attractive target for the development of drugs to treat this disease. A series of penicillin conjugates, in which 6-aminopenicillanic acid was acylated with aromatic acid chlorides, has been prepared and assayed against pig PAP. The binding mode of most of these conjugates is purely competitive, and some members of this class have potencies comparable to the best PAP inhibitors yet reported. The structurally related penicillin G was shown to be neither an inhibitor nor a substrate for pig PAP. Molecular modelling has been used to examine the binding modes of these compounds in the active site of the enzyme and to rationalise their activities.
