Docking studies of 4-phenylthiazolinethione on human IDO1 suggest complexation of the heme iron by the exocyclic sulfur atom further reinforced by hydrophobic interactions of the phenyl ring within pocket A of the enzyme. On this basis, chemical modifications were proposed to increase inhibition activity. Synthetic routes had to be adapted and optimized to yield the desired substituted 4- and 5-arylthiazolinethiones. Their biological evaluation shows that 5-aryl regioisomers are systematically less potent than the corresponding 4-aryl analogs. Substitution on the phenyl ring does not significantly increase inhibition potency, except for 4-Br and 4-Cl derivatives.
- 4-Phenyl thiazolinethione
- Aryl-thiazoline thione
- IDO inhibition
- Indoleamine 2,3-dioxygenase (IDO)
- Indoleamine-Pyrrole 2,3,-Dioxygenase/antagonists & inhibitors
- Thiones/chemical synthesis
- Thiazolidines/chemical synthesis
- Structure-Activity Relationship
- Molecular Docking Simulation
- Enzyme Inhibitors/chemical synthesis
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Technological Platform Physical Chemistry and characterization
Facility/equipment: Technological Platform