FL47

FL47 binds recombinant human FEM1B (residues 1−356) with submicromolar affinity (IC₅₀ = 0.96 μM) via dual-site interactions, including noncovalent contacts with key site A residues and covalent modification of Cys186 at site C^[1].
FL47 binds recombinant human FEM1B in a MST assay, with binding dependent on the same key residues (W93, S122, N151, N155, C186) identified in FP assays^[1].
FL47 forms a stable covalent complex with FEM1B over a 200 ns MD simulation, with an average MM-GBSA binding free energy of −51.2 kcal/mol, mediated by specific dual-site noncovalent and covalent interactions^[1].
FL47 (10-20 μM; 12 h) stabilizes the FNIP1 degron reporter in HEK293T cells in a FEM1B-dependent manner^[1].
FL47 directly binds endogenous FEM1B in HEK293T cells, as demonstrated by competitive displacement of a biotinylated FL47 probe in streptavidin pull-down assays^[1].
FL47 (50 μM; 3 h) engages FEM1B in HEK293 cells, as shown by thermal stabilization of the protein^[1].
FL47 (up to 25 μM; 72 h) shows markedly reduced cytotoxicity toward HEK293T cells compared to EN106, with no measurable CC₅₀ at concentrations up to 25 μM^[1].