ArticleChemistry & biodiversity2026
Exploring Non-Covalent Pin1-PROTACs Insights Into Degradation Efficiency in Multiple Myeloma Cell Line.
Article in Chemistry & biodiversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Pin1 is a peptidyl-prolyl isomerase involved in key signalling pathways and upregulated in different cancers, including Multiple Myeloma (MM), where it is linked to poor prognosis/drug resistance. Despite its therapeutic relevance, Pin1 remains challenging to target with conventional inhibitors thereby motivating interest in Targeted Protein Degradation (TPD) strategies. All reported Pin1-PROTACs rely on covalent Pin1 ligands, leaving non-covalent degraders largely unexplored. Since PROTACs (PROteolysis TArgeting Chimeras) act catalytically/reversibly, non-covalent designs are attractive. Here, we describe the design/synthesis/evaluation of 12 non-covalent potential Pin1-PROTACs (P1-P12) based on reversible peptidomimetic ligand and in a prodrug form to allow cell permeability. Despite rational design, stability and measurable target engagement, P1-P12 displayed none or very limited degradation activity, with the most active molecule, P3, achieving only 39% of Pin1 depletion in MM cells. To confirm Pin1 degradability in MM, MM1.R cells were treated with the covalent PROTAC P1D-34, which induced robust dose-dependent degradation (DC
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