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A Novel Anti-Cancer/Anti-Proliferation and Anti-Migration Compound—An Inhibitor to Dual Specificity Phosphatase Slingshot-2

Technology Benefits

Highly specific SSH-2 inhibitor that regulates F-actin depolymerization.

Technology Application

New therapeutics, targeting actin filament dynamics and signaling pathways, for the treatment of cancer, Alzheimer’s, and other diseases.

Detailed Technology Description

Scientists at UC San Diego have found a family of small molecule inhibitors that specifically binds to SSH-2. These compounds represent the first inhibitors of a phosphatase that regulates the F-actin depolymerization.The inventors used a molecular docking simulation software (DOCK 6.0) to virtually screen open-source chemical databases and determined the binding affinities to 18 of DSPs with known three-dimensional structures as determined by x-ray crystallography, including SSH-2, VHR (DUSP3), VHY (DUSP15), VHZ (DUSP23), VH1 (DUSP12), VH3 (DUSP5), PTEN (phosphatase and tensin homolog), KAP (Cdk2 associated protein phosphatase), MKP3 (rVH6, Pyst1), MKP4, MKP5, MTMR2, DUSP18, PRL3, CDC14b, Pac-1, Jsp-1, and TMPD. Five compounds with similar chemical structures have the highest affinity for SSH-2, but lowest affinity for the other DSPs, among the best 100 SSH-2 binding compounds. Figure 1. Diagram illustrating the role of phosphorylation and SSH-2 in actin filament assembly.

Industry

Disease Diagnostic/Treatment

Sub Group

Cancer/Tumor

Application No.

9487522

Others

State Of Development

Virtual screening yielded a compound with high binding affinity to SSH-2 and very low binding affinity to other DSPs.

Related Materials

Mui MK , Levesque MJ, Chien S, and Haga JH. In-Silico Identification of High Potential SSH-2 Specific Inhibitors. The FASAB J. (1_MeetingAbstracts) Apr 2010; 24 No. 1060.3.

Tech ID/UC Case