In the past, MGDs have been discovered serendipitously. The rational design of MGDs has been extremely challenging due to the complexity of ternary structure formed by E3 ligase, MGD, and protein substrate (target).
Most MGD development efforts are based on IMiDs' (e.g. lenalidomide) core chemical structure, which leads to limited number of MGD targets and poor lP protection.
A biology-backed glue library that includes >10,000 structurally differentiated MGD compounds with associated compound-induced proximity and degradation data.
Comprehensive MGD screening and validation systems.
Large proprietary degradation and proximity data sets for Al/Machine learning.
In the past, MGDs have been discovered serendipitously. The rational design of MGDs has been extremely challenging due to the complexity of ternary structure formed by E3 ligase, MGD, and protein substrate (target).
Most MGD development efforts are based on IMiDs' (e.g. lenalidomide) core chemical structure, which leads to limited number of MGD targets and poor lP protection.
A biology-backed glue library that includes >10,000 structurally differentiated MGD compounds with associated compound-induced proximity and degradation data.
Comprehensive MGD screening and validation systems.
Large proprietary degradation and proximity data sets for Al/Machine learning.



Most MGD development efforts are based on IMiDs' (e.g. lenalidomide) core chemical structure, which leads to limited number of MGD targets and poor lP protection. Degron has built an unique MGD library based on novel scaffold chemistry. The glue library now includes >10,000 structurally differentiated MGD compounds, with associated compound-induced proximity and degradation data, and is quickly expanding.
Degron has generated large compound-induced proximity and degradation data sets. In addition to producing first-in-class pipeline programs, this proprietary data broadens our understanding on potential MGD target proteins and supports MGD discovery collaborations with industry partners.
MGDs of selected targets are discovered by library screening, glue mechanism of action validation and compound optimization.
HuR (Human antigen R) is a previously undruggable RNA-binding protein playing critical roles in driving cancer, inflammation and metabolic disorders. HuR is over-expressed or cytoplasmic enriched in many cancers particularly in response to stresses including oncogenic mutations and chemo or targeted therapies. HuR is also a well-studied target in inflammatory diseases such as pancreatitis, rheumatoid arthritis, and neuroinflammation. HuR is considered “undruggable” by conventional approaches. Multiple modalities (RNAi, small molecule inhibitors of translocation, dimerization or RNA binding) have been investigated to target this protein but none has advanced beyond preclinical stage due to various technical challenges. DEG6498 is a potent and orally bioavailable small molecule molecular glue degrader that induces the interaction between the E3 ubiquitin ligase component cereblon (CRBN) and HuR, leading to the targeted degradation of the HuR protein. In January 2025, Degron received FDA IND clearance for DEG6498 to initiate clinical development in solid tumors. The study will assess its safety, tolerability, pharmacokinetics, pharmacodynamics, and anti-tumor activity across multiple types of solid tumors.
WEE1 kinase phosphorylates and inhibits CDK1 and CDK2 to coordinate cell cycle arrest with DNA damage response. WEE1 molecular glue degrader exhibits a differentiated mechanism of action compared to conventional WEE1 inhibitors. The preclinical candidate is expected to be selected in 1H 2025.
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