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Rational design and in vitro HDAC inhibitory profiling of SDFZ‐8 . (A) Structure‐based design of new HDAC inhibitors using fragment‐centric topographic mapping strategy. The favorable binding mode of SDFZ‐8 was predicted using Glide. The lead compounds WL‐9w and CC‐4a were presented as tan and gray molecules in the active site of HDAC1 (PDB: 5ICN). The transparent spheres represent pockets that are detected by AlphaSpace . The alpha‐atoms clusters in each pocket were presented as small spheres with different colors. The unoccupied pockets were marked with a red cycle. The images were illustrated by UCSF Chimera. (B) The chemical structure and HDAC inhibitory activities of the quinoline derivatives were determined by HeLa extract. Results are expressed as the mean ± SD of three separate determinations. (C) The HDAC inhibition curve of selected compounds at different concentrations of three separate determinations. (D) Western blotting analysis of MDA‐MB‐231 cells incubated with selected compounds (µM) for 24 h. (E) Immunofluorescence of ac‐H3 in MDA‐MB‐231 cells incubated with 1 µM selected compounds for 24 h.

Journal: MedComm

Article Title: Preclinical Characterization of SDFZ‐8, a Highly Potent HDAC1 Inhibitor, for Cancer Immunotherapy

doi: 10.1002/mco2.70500

Figure Lengend Snippet: Rational design and in vitro HDAC inhibitory profiling of SDFZ‐8 . (A) Structure‐based design of new HDAC inhibitors using fragment‐centric topographic mapping strategy. The favorable binding mode of SDFZ‐8 was predicted using Glide. The lead compounds WL‐9w and CC‐4a were presented as tan and gray molecules in the active site of HDAC1 (PDB: 5ICN). The transparent spheres represent pockets that are detected by AlphaSpace . The alpha‐atoms clusters in each pocket were presented as small spheres with different colors. The unoccupied pockets were marked with a red cycle. The images were illustrated by UCSF Chimera. (B) The chemical structure and HDAC inhibitory activities of the quinoline derivatives were determined by HeLa extract. Results are expressed as the mean ± SD of three separate determinations. (C) The HDAC inhibition curve of selected compounds at different concentrations of three separate determinations. (D) Western blotting analysis of MDA‐MB‐231 cells incubated with selected compounds (µM) for 24 h. (E) Immunofluorescence of ac‐H3 in MDA‐MB‐231 cells incubated with 1 µM selected compounds for 24 h.

Article Snippet: In detail, the HeLa nuclear extract, HDAC1 (BPS BIOSCIENCE INC, 50051), HDAC2 (BPS BIOSCIENCE Inc; 50052), HDAC3/NCOR1 complex (BPS BIOSCIENCE Inc; 50003), HDAC4 (BPS BIOSCIENCE Inc; 50004), HDAC5 (BPS BIOSCIENCE Inc; 50005), HDAC6 (BPS BIOSCIENCE Inc; 50006), HDAC7 (BPS BIOSCIENCE Inc; 50007), HDAC8 (BPS BIOSCIENCE Inc; 50008), HDAC9 (BPS BIOSCIENCE Inc; 50009), HDAC10 (BPS BIOSCIENCE Inc; 50010), or HDAC11 (BPS BIOSCIENCE Inc; 50011) was diluted to the proper concentrations according to the relative enzymatic activity and the linear range of the plate reader and mixed with different concentrations of drugs.

Techniques: In Vitro, Binding Assay, Inhibition, Western Blot, Incubation, Immunofluorescence

SDFZ‐8 promotes immune activation and synergizes with anti‐PD‐L1 therapy in the MC38 model. (A–C) Impacts of HDAC1 inhibition on PD‐L1 expression in MDA‐MB‐231 cells and knockdown of HDAC1 using shRNA virus infected for 96 h. (D) Treatment with the HDAC1 inhibitor SDFZ‐8 for 24 h upregulates PD‐L1 expression in MC38 cells of four separate determinations ( n = 4/each group). (E) In vivo antitumor potency of SDFZ‐8 in the MC38 syngeneic model ( n = 5/each group). (F) Comparison of the tumor growth suppression and PD‐L1 regulation between SAHA and SDFZ‐8 in combination with anti‐PD‐L1 blockade ( n = 6/each group). (**** p < 0.0001, ** p < 0.01, * p < 0.05 vs. vehicle; ## p < 0.01, # p < 0.05 vs. SDFZ‐8 ).

Journal: MedComm

Article Title: Preclinical Characterization of SDFZ‐8, a Highly Potent HDAC1 Inhibitor, for Cancer Immunotherapy

doi: 10.1002/mco2.70500

Figure Lengend Snippet: SDFZ‐8 promotes immune activation and synergizes with anti‐PD‐L1 therapy in the MC38 model. (A–C) Impacts of HDAC1 inhibition on PD‐L1 expression in MDA‐MB‐231 cells and knockdown of HDAC1 using shRNA virus infected for 96 h. (D) Treatment with the HDAC1 inhibitor SDFZ‐8 for 24 h upregulates PD‐L1 expression in MC38 cells of four separate determinations ( n = 4/each group). (E) In vivo antitumor potency of SDFZ‐8 in the MC38 syngeneic model ( n = 5/each group). (F) Comparison of the tumor growth suppression and PD‐L1 regulation between SAHA and SDFZ‐8 in combination with anti‐PD‐L1 blockade ( n = 6/each group). (**** p < 0.0001, ** p < 0.01, * p < 0.05 vs. vehicle; ## p < 0.01, # p < 0.05 vs. SDFZ‐8 ).

Article Snippet: In detail, the HeLa nuclear extract, HDAC1 (BPS BIOSCIENCE INC, 50051), HDAC2 (BPS BIOSCIENCE Inc; 50052), HDAC3/NCOR1 complex (BPS BIOSCIENCE Inc; 50003), HDAC4 (BPS BIOSCIENCE Inc; 50004), HDAC5 (BPS BIOSCIENCE Inc; 50005), HDAC6 (BPS BIOSCIENCE Inc; 50006), HDAC7 (BPS BIOSCIENCE Inc; 50007), HDAC8 (BPS BIOSCIENCE Inc; 50008), HDAC9 (BPS BIOSCIENCE Inc; 50009), HDAC10 (BPS BIOSCIENCE Inc; 50010), or HDAC11 (BPS BIOSCIENCE Inc; 50011) was diluted to the proper concentrations according to the relative enzymatic activity and the linear range of the plate reader and mixed with different concentrations of drugs.

Techniques: Activation Assay, Inhibition, Expressing, Knockdown, shRNA, Virus, Infection, In Vivo, Comparison