Activation and inhibition of the proteasome by betulinic acid and its derivatives.

Published

Journal Article

This study discovered that betulinic acid (BA) is a potent proteasome activator that preferentially activates the chymotrypsin-like activity of the proteasome. Chemical modifications can transform BA into proteasome inhibitors. Chemical modifications at the C-3 position of BA resulted in compounds, such as dimethylsuccinyl BA (DSB), with various inhibitory activities against the human 20S proteasome. Interestingly, the proteasomal activation by BA and the inhibitory activity of DSB could be abrogated by introducing a side chain at the C-28 position. In summary, this study discovered a class of small molecules that can either activate or inhibit human proteasome activity depending on side chain modifications.

Full Text

Duke Authors

Cited Authors

  • Huang, L; Ho, P; Chen, C-H

Published Date

  • October 16, 2007

Published In

Volume / Issue

  • 581 / 25

Start / End Page

  • 4955 - 4959

PubMed ID

  • 17904555

Pubmed Central ID

  • 17904555

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2007.09.031

Language

  • eng

Conference Location

  • England