Work

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

Year: 2007

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2007.09.031

Authors: Li Huang, Phong Ho, Chin-Ho Chen

Institution: Duke Medical Center

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of Allergy and Infectious Diseases

Awards: G2971678537, Betulinic acid derivatives as anti-HIV agents, Dynamic envelope interactions and HIV-1 neutralization., G6487473806