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Title:
Discovery of novel IDO1 inhibitors via structure-based virtual screening and biological assays | Journal of Computer-Aided Molecular Design
Description:
Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. IDO1 has been proven to be an attractive target for many diseases, such as breast cancer, lung cancer, colon cancer, prostate cancer, etc. In this study, docking-based virtual screening and bioassays were conducted to identify novel inhibitors of IDO1. The cellular assay demonstrated that 24 compounds exhibited potent inhibitory activity against IDO1 at micromolar level, including 8 compounds with IC50 values below 10 μM and the most potent one (compound 1) with IC50 of 1.18 ± 0.04 μM. Further lead optimization based on similarity searching strategy led to the discovery of compound 28 as an excellent inhibitor with IC50 of 0.27 ± 0.02 μM. Then, the structure–activity relationship of compounds 1, 2, 8 and 14 analogues is discussed. The interaction modes of two compounds against IDO1 were further explored through a Python Based Metal Center Parameter Builder (MCPB.py) molecular dynamics simulation, binding free energy calculation and electrostatic potential analysis. The novel IDO1 inhibitors of compound 1 and its analogues could be considered as promising scaffold for further development of IDO1 inhibitors.
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Keywords {🔍}
pubmed, article, google, scholar, cas, chem, ido, wang, indoleamine, dioxygenase, inhibitors, cancer, molecular, med, central, screening, liu, discovery, virtual, yao, sun, hou, phys, zhang, mol, study, inhibitor, dynamics, free, comput, design, based, energy, mmgbsa, research, structurebased, zhao, compounds, potent, simulation, binding, calculation, inhibition, drug, tian, immune, lee, methods, calculations, mmpbsa,
Topics {✒️}
docking-based virtual screening month download article/chapter high-content drug screening structure-based virtual screening il-6/stat3/pd-l1 pathway small molecules binding mm/gbsa methodologies evaluated 3-dioxygenase-initiated l-tryptophan metabolism combining virtual screening igf-ii/igf2r recognition molecular dynamics simulations opls-aa force field tumor-infiltrating immune cells msi-high colon cancer drug target 27 mm/gbsa methods 3 mm/gbsa methods 1 free energy simulations essential subunit pa-pb1 active site-inhibitor interactions full article pdf structure-activity relationship study drug resistance mechanism molecular dynamics simulation ido1 inhibitor screening visual molecular dynamics concentration-dependent inhibition free-energy calculation free energy calculation epithelial-mesenchymal transition cheatham te 3rd privacy choices/manage cookies molecular modeling perspective case da molecular modeling studies structure–activity relationship avoid immune detection mcgee td jr inhibitor design revealed quantum chemical calculations free energy studies structure-activity relationships merz km jr quantum mechanics calculations mouse melanoma model article ge structure−activity study immune suppressive enzyme hydration free energies molecular dynamics
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headline:Discovery of novel IDO1 inhibitors via structure-based virtual screening and biological assays
description:Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. IDO1 has been proven to be an attractive target for many diseases, such as breast cancer, lung cancer, colon cancer, prostate cancer, etc. In this study, docking-based virtual screening and bioassays were conducted to identify novel inhibitors of IDO1. The cellular assay demonstrated that 24 compounds exhibited potent inhibitory activity against IDO1 at micromolar level, including 8 compounds with IC50 values below 10 μM and the most potent one (compound 1) with IC50 of 1.18 ± 0.04 μM. Further lead optimization based on similarity searching strategy led to the discovery of compound 28 as an excellent inhibitor with IC50 of 0.27 ± 0.02 μM. Then, the structure–activity relationship of compounds 1, 2, 8 and 14 analogues is discussed. The interaction modes of two compounds against IDO1 were further explored through a Python Based Metal Center Parameter Builder (MCPB.py) molecular dynamics simulation, binding free energy calculation and electrostatic potential analysis. The novel IDO1 inhibitors of compound 1 and its analogues could be considered as promising scaffold for further development of IDO1 inhibitors.
datePublished:2021-04-27T00:00:00Z
dateModified:2021-04-27T00:00:00Z
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IDO1 inhibitor
Virtual screening
Molecular docking
Molecular dynamics simulations
MM-GBSA calculation
Physical Chemistry
Computer Applications in Chemistry
Animal Anatomy / Morphology / Histology
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description:Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. IDO1 has been proven to be an attractive target for many diseases, such as breast cancer, lung cancer, colon cancer, prostate cancer, etc. In this study, docking-based virtual screening and bioassays were conducted to identify novel inhibitors of IDO1. The cellular assay demonstrated that 24 compounds exhibited potent inhibitory activity against IDO1 at micromolar level, including 8 compounds with IC50 values below 10 μM and the most potent one (compound 1) with IC50 of 1.18 ± 0.04 μM. Further lead optimization based on similarity searching strategy led to the discovery of compound 28 as an excellent inhibitor with IC50 of 0.27 ± 0.02 μM. Then, the structure–activity relationship of compounds 1, 2, 8 and 14 analogues is discussed. The interaction modes of two compounds against IDO1 were further explored through a Python Based Metal Center Parameter Builder (MCPB.py) molecular dynamics simulation, binding free energy calculation and electrostatic potential analysis. The novel IDO1 inhibitors of compound 1 and its analogues could be considered as promising scaffold for further development of IDO1 inhibitors.
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