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SML1573

Sigma-Aldrich

Tolrestat

≥98% (HPLC)

Synonym(s):

AY-27773, CID 53359, N-[[5 -(Trifluoromethyl)-6-methoxy-lnaphthalenyl]thioxomethyl]-N-methylglycine, N-[[6-Methoxy-5-(trifluoromethyl)-1-naphthalenyl]thioxomethyl]-N-methyl-glycine, Tolrestatin

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About This Item

Empirical Formula (Hill Notation):
C16H14F3NO3S
CAS Number:
Molecular Weight:
357.35
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

Assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 20 mg/mL, clear

storage temp.

2-8°C

InChI

1S/C16H14F3NO3S/c1-20(8-13(21)22)15(24)11-5-3-4-10-9(11)6-7-12(23-2)14(10)16(17,18)19/h3-7H,8H2,1-2H3,(H,21,22)

InChI key

LUBHDINQXIHVLS-UHFFFAOYSA-N

Biochem/physiol Actions

Tolrestat is an orally active and potent aldose reductase inhibitor. Studies have also shown that it reduces RBC (red blood cells) sorbitol levels in rats.
Tolrestat is considered to be effective in treating the consequences of diabetes including neuropathy, nephropathy, retinopathy and esophageal motility and vibration perception. Tolrestat is also believed to have lesser or no toxic effects.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

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Effect of Tolrestat on oesophageal transit time and cholecystic motility in type 2 diabetic patients with asymptomatic diabetic neuropathy.
Fabiani F, et al.
Diabete & Metabolisme, 21(5), 360-364 (1995)
Principles of diabetes mellitus (2010)
Felicia D'Andrea et al.
Journal of enzyme inhibition and medicinal chemistry, 35(1), 1194-1205 (2020-05-13)
Aldose reductase is a key enzyme in the development of long term diabetic complications and its inhibition represents a viable therapeutic solution for people affected by these pathologies. Therefore, the search for effective aldose reductase inhibitors is a timely and
Susanna Nencetti et al.
Bioorganic & medicinal chemistry, 25(12), 3068-3076 (2017-04-11)
Aldose reductase (ALR2), a NADPH-dependent reductase, is the first and rate-limiting enzyme of the polyol pathway of glucose metabolism and is implicated in the pathogenesis of secondary diabetic complications. In the last decades, this enzyme has been targeted for inhibition

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