SML3236
UNC10201652
≥98 mg/mL (HPLC)
Synonym(s):
4-(8-(piperazin-1-yl)-1,2,3,4-tetrahydro-[1,2,3]triazino[4′,5′:4,5]thieno[2,3-c]isoquinolin-5-yl)morpholine, 1,2,3,4-Tetrahydro-5-(4-morpholinyl)-8-(1-piperazinyl)[1,2,3]triazino[4′,5′:4,5]thieno[2,3-c]isoquinoline
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About This Item
Empirical Formula (Hill Notation):
C20H25N7OS
CAS Number:
Molecular Weight:
411.52
UNSPSC Code:
12352107
NACRES:
NA.77
Form:
powder
Quality level:
InChI key
ZPVQONCMKZBGTB-UHFFFAOYSA-N
SMILES string
C12=C(N3CCOCC3)N=C(SC4=C5N=NN=C4N6CCNCC6)C5=C1CCCC2
form
powder
concentration
≥98 mg/mL (HPLC)
color
white to beige
solubility
DMSO: 2 mg/mL, clear
storage temp.
2-8°C
Quality Level
Related Categories
General description
UNC10201652 is a potent and substrate-dependent slow-binding inhibitor of bacterial β-glucuronidases (GUSs) in the gut. UNC10201652 appears to target a catalytic intermediate. It alleviates irinotecan-induced gut damage in mouse models of cancer.
Biochem/physiol Actions
potent and selective slow binding inhibitor microbiome β-glucuronidase enzyme
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Aadra P Bhatt et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(13), 7374-7381 (2020-03-15)
Irinotecan treats a range of solid tumors, but its effectiveness is severely limited by gastrointestinal (GI) tract toxicity caused by gut bacterial β-glucuronidase (GUS) enzymes. Targeted bacterial GUS inhibitors have been shown to partially alleviate irinotecan-induced GI tract damage and
Samuel J Pellock et al.
ACS central science, 4(7), 868-879 (2018-08-01)
Microbial β-glucuronidases (GUSs) cause severe gut toxicities that limit the efficacy of cancer drugs and other therapeutics. Selective inhibitors of bacterial GUS have been shown to alleviate these side effects. Using structural and chemical biology, mass spectrometry, and cell-based assays
Kristen A Biernat et al.
Scientific reports, 9(1), 825-825 (2019-01-31)
Bacterial β-glucuronidase (GUS) enzymes cause drug toxicity by reversing Phase II glucuronidation in the gastrointestinal tract. While many human gut microbial GUS enzymes have been examined with model glucuronide substrates like p-nitrophenol-β-D-glucuronide (pNPG), the GUS orthologs that are most efficient
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