Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase

Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase

Thymidine phosphorylase is an enzyme involved in pyrimidine salvage pathway that is identical to platelet-derived endothelial cell growth factor (PD-ECGF) and gliostatin. It is enormously up regulated in a variety of solid tumors. Furthermore, surpassing of TP level prot...

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Published in:Bioorganic Chemistry
Main Author: Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
Format: Article
Language:English
Published: Academic Press Inc. 2018
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85047345848&doi=10.1016%2fj.bioorg.2018.05.011&partnerID=40&md5=1382efb7b09ea9d905d04f2b7d6cf11a
id 2-s2.0-85047345848
spelling 2-s2.0-85047345848
Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
2018
Bioorganic Chemistry
79

10.1016/j.bioorg.2018.05.011
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85047345848&doi=10.1016%2fj.bioorg.2018.05.011&partnerID=40&md5=1382efb7b09ea9d905d04f2b7d6cf11a
Thymidine phosphorylase is an enzyme involved in pyrimidine salvage pathway that is identical to platelet-derived endothelial cell growth factor (PD-ECGF) and gliostatin. It is enormously up regulated in a variety of solid tumors. Furthermore, surpassing of TP level protects tumor cells from apoptosis and helps cell survival. Thus TP is identified as a prime target for developing novel anticancer therapies. A new class of exceptionally potent isatin based oxadiazole (1–30) has been synthesized and evaluated for thymidine phosphorylase inhibitory potential. All analogs showed potent thymidine phosphorylase inhibition when compared with standard 7-Deazaxanthine, 7DX (IC 50 = 38.68 ± 1.12 µM). Molecular docking study was performed in order to determine the binding interaction of these newly synthesized compounds, which revealed that these synthesized compounds established stronger hydrogen bonding network with active site of residues as compare to the standard compound 7DX. © 2018 Elsevier Inc.
Academic Press Inc.
452068
English
Article
author Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
spellingShingle Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
author_facet Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
author_sort Javid M.T.; Rahim F.; Taha M.; Nawaz M.; Wadood A.; Ali M.; Mosaddik A.; Shah S.A.A.; Farooq R.K.
title Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
title_short Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
title_full Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
title_fullStr Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
title_full_unstemmed Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
title_sort Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase
publishDate 2018
container_title Bioorganic Chemistry
container_volume 79
container_issue
doi_str_mv 10.1016/j.bioorg.2018.05.011
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-85047345848&doi=10.1016%2fj.bioorg.2018.05.011&partnerID=40&md5=1382efb7b09ea9d905d04f2b7d6cf11a
description Thymidine phosphorylase is an enzyme involved in pyrimidine salvage pathway that is identical to platelet-derived endothelial cell growth factor (PD-ECGF) and gliostatin. It is enormously up regulated in a variety of solid tumors. Furthermore, surpassing of TP level protects tumor cells from apoptosis and helps cell survival. Thus TP is identified as a prime target for developing novel anticancer therapies. A new class of exceptionally potent isatin based oxadiazole (1–30) has been synthesized and evaluated for thymidine phosphorylase inhibitory potential. All analogs showed potent thymidine phosphorylase inhibition when compared with standard 7-Deazaxanthine, 7DX (IC 50 = 38.68 ± 1.12 µM). Molecular docking study was performed in order to determine the binding interaction of these newly synthesized compounds, which revealed that these synthesized compounds established stronger hydrogen bonding network with active site of residues as compare to the standard compound 7DX. © 2018 Elsevier Inc.
publisher Academic Press Inc.
issn 452068
language English
format Article
accesstype
record_format scopus
collection Scopus
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