Unknown

Dataset Information

0

Structural Optimization and Structure-Activity Relationship of 4-Thiazolidinone Derivatives as Novel Inhibitors of Human Dihydroorotate Dehydrogenase.


ABSTRACT: Human dihydroorotate dehydrogenase (hDHODH), one of the attractive targets for the development of immunosuppressive drugs, is also a potential target of anticancer drugs and anti-leukemic drugs. The development of promising hDHODH inhibitors is in high demand. Based on the unique binding mode of our previous reported 4-thiazolidinone derivatives, via molecular docking method, three new series 4-thiazolidinone derivatives were designed and synthesized as hDHODH inhibitors. The preliminary structure-activity relationship was investigated. Compound 9 of biphenyl series and compound 37 of amide series displayed IC50 values of 1.32 ?M and 1.45 ?M, respectively. This research will provide valuable reference for the research of new structures of hDHODH inhibitors.

SUBMITTER: Zeng F 

PROVIDER: S-EPMC6696179 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural Optimization and Structure-Activity Relationship of 4-Thiazolidinone Derivatives as Novel Inhibitors of Human Dihydroorotate Dehydrogenase.

Zeng Fanxun F   Quan Lina L   Yang Guantian G   Qi Tiantian T   Zhang Letian L   Li Shiliang S   Li Honglin H   Zhu Lili L   Xu Xiaoyong X  

Molecules (Basel, Switzerland) 20190731 15


Human dihydroorotate dehydrogenase (<i>h</i>DHODH), one of the attractive targets for the development of immunosuppressive drugs, is also a potential target of anticancer drugs and anti-leukemic drugs. The development of promising <i>h</i>DHODH inhibitors is in high demand. Based on the unique binding mode of our previous reported 4-thiazolidinone derivatives, via molecular docking method, three new series 4-thiazolidinone derivatives were designed and synthesized as <i>h</i>DHODH inhibitors. Th  ...[more]

Similar Datasets

| S-EPMC6071797 | biostudies-literature
| S-EPMC6099574 | biostudies-literature
| S-EPMC3156099 | biostudies-literature
| S-EPMC4018051 | biostudies-literature
| S-EPMC5997609 | biostudies-literature
| S-EPMC3124361 | biostudies-literature
| S-EPMC4595849 | biostudies-literature
| S-EPMC6120730 | biostudies-literature
| S-EPMC4595722 | biostudies-literature
| S-EPMC7435507 | biostudies-literature