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SHP2-D26
- Development stage
- Preclinical
- Lead developer
- University of Michigan
- Modality
- PROTACs (E3 ligase recruitment) → Targeted Protein Degraders (TPDs) → Small Molecules, Bivalent/Multivalent Binders → Multivalent & Scaffold-Based Small Molecules → Small Molecules
- Administration
- Intraperitoneal, Intravenous
01
Overview
SHP2-D26 is a first-in-class, potent proteolysis-targeting chimera (PROTAC) degrader that targets Src homology-2 domain-containing phosphatase 2 (SHP2) for ubiquitin-proteasome-mediated degradation. Developed by the University of Michigan, SHP2-D26 simultaneously binds SHP2 and the von Hippel-Lindau (VHL) E3 ubiquitin ligase, inducing proximity-driven ubiquitination and subsequent proteasomal degradation of SHP2. This leads to the sustained suppression of downstream RAS-MAPK signaling, such as ERK phosphorylation. SHP2-D26 has been investigated in preclinical studies for the treatment of various cancers, including esophageal cancer, acute myeloid leukemia (AML), and non-small cell lung cancer (NSCLC), as well as inflammatory and degenerative joint diseases like rheumatoid arthritis and osteoarthritis.
- Other names
- SHP2 D26SHP-2 D26SHP 2 D26
02
Targets
PTPN11 (Tyrosine-protein phosphatase non-receptor type 11)VHL (Von Hippel–Lindau tumor suppressor protein)
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