Hexylitaconic acid: a new inhibitor of p53-HDM2 interaction isolated from a marine-derived fungus, Arthrinium sp.
A new inhibitor of p53-HDM2 interaction was isolated from a culture of marine-derived fungus, Arthrinium sp. The structure was identified to be (-)-hexylitaconic acid (1) by spectroscopic analysis. The inhibition of p53-HDM2 binding was tested by the ELISA method, and 1 inhibited the binding with an IC(50) value of 50 microg/mL. Although a number of synthetic inhibitors of p53-HDM2 interaction have been reported so far, 1 is the second inhibitor isolated from natural resources.
Tsukamoto
Sachiko
S
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa 920-1192, Japan. sachiko@p.kanazawa-u.ac.jp
Yoshida
Takushi
T
Hosono
Hidetaka
H
Ohta
Tomihisa
T
Yokosawa
Hideyoshi
H
D001203:Ascomycota / Q000378:metabolism*; D002626:Chemistry, Pharmaceutical / Q000379:methods*; D018360:Crystallography, X-Ray; D004305:Dose-Response Relationship, Drug; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004797:Enzyme-Linked Immunosorbent Assay; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D020128:Inhibitory Concentration 50; D008956:Models, Chemical; D011485:Protein Binding; D051736:Proto-Oncogene Proteins c-mdm2 / Q000378:metabolism*; D013386:Succinates / Q000737:chemistry*; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
C426868:2-methylene-3-hexylbutanedioic acid; D004791:Enzyme Inhibitors; D005656:Fungal Proteins; D013386:Succinates; D016159:Tumor Suppressor Protein p53; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2