Benzimidazolone as potent chymase inhibitor: Modulation of reactive metabolite formation in the hydrophobic (P1) region
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Acknowledgment
The authors would like to thank Dr. Anil Padyana for the deposition of X-ray crystal coordinates.
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Design and synthesis of new N-substituted benzimidazolidinone as predicted human BRD4 and human chymase inhibitors via molecular docking studies
2023, Journal of Molecular StructureStructure-based virtual screening for novel chymase inhibitors by in silico fragment mapping
2019, Journal of Molecular Graphics and ModellingCitation Excerpt :Because these proteins contribute to adverse cardiac remodeling after myocardial infarction [7], pharmaceutical development of chymase inhibitors has primarily focused on cardiovascular indications [8–16]. To date, a variety of small molecule chymase inhibitors have been identified and their mode of binding at the active site of the enzyme determined [17–23]. However, no chymase inhibitor has been used for clinical applications.
Dissecting the role of mutations in chymase inhibition: Free energy and decomposition analysis
2017, GeneCitation Excerpt :In the present study we performed mutations and molecular dynamics simulation of wild and two single mutants Arg143Gln and Lys192Met. PDB ID 2HVX contains an inhibitor [(1s)-1-(5-Chloro-1-Benzothien-3-yl)-2-(2-napthylamino)-2-oxoethyl] Phosphonic Acid (Greco et al. 2007) (designated as Phosphonic Acid inhibitor in the rest part of the manuscript) and PDB ID 3S0N contains a benzimidazolone inhibitor at the active site of chymase (Greco et al. 2007; Lo et al. 2011), were used for the study. In the previous study Ahooghalandari et al. (2013) performed in-vitro study to demonstrate the effect of these mutations on the binding of Phosphonic Acid inhibitor.
Expression of recombinant human mast cell chymase with Asn-linked glycans in glycoengineered Pichia pastoris
2014, Protein Expression and PurificationCitation Excerpt :A high-yield source of active rhChymase with human-type glycosylation would facilitate chymase research by providing a better alternative to chymase from human tissues. Human chymase contains glycans at two Asn-linked glycosylation sites (Asn-72 and Asn-95) [20,27,42–45]; however, no studies to date have demonstrated the composition of these glycans. Some researchers indicate that human chymase may actually include sub-types that vary in tissue localization, glycan composition, and heparin binding affinity [46,47].
Crystal structure of a complex of human chymase with its benzimidazole derived inhibitor
2013, Journal of Synchrotron Radiation
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Present address: Karos Pharmaceuticals.