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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.
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Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.

Journal: Frontiers in Oncology

Article Title: Targeting MEST using cobicistat as a therapeutic strategy for gastric cancer through suppressing NF-κB signaling

doi: 10.3389/fonc.2026.1901635

Figure Lengend Snippet: Cobicistat was identified as a novel MEST inhibitor. (A) Eight binding pockets of MEST were identified using the SiteFinder module of MOE software. (B) Virtual docking screening of MEST inhibitor from a library. (C) A preliminary screening of 36 compounds was performed by SPR. (D) Binding affinity of the cobicistat to human MEST assessed by SPR. (E) Molecular structure of cobicistat small molecule. (F) Computational model and the interaction of cobicistat with MEST complex. (G) The interacting amino acids and hydrogen bonds between the complexes.

Article Snippet: Here, we identified a candidate MEST-inhibitory compound, cobicistat, by screening the TargetMol and Selleck small-molecule compound libraries based on its catalytic site, ASN163.

Techniques: Binding Assay, Software, Docking Assay, Screening