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1286275-72-6

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1286275-72-6 Usage

General Description

"Tert-butyl 1-(4-chlorobenzyl)piperidin-4-ylcarbamate" is a chemical compound that contains a carbamate functional group and a piperidine ring. The tert-butyl group and the chlorobenzyl group are both attached to the piperidine ring. The presence of the carbamate group suggests that it may have uses in medicinal chemistry, potentially as a pharmaceutical intermediate or as a building block for the synthesis of other compounds. Additionally, the chlorobenzyl group may confer specific properties or reactivity to the compound. Further investigation and analysis would be needed to determine its exact applications and potential uses.

Check Digit Verification of cas no

The CAS Registry Mumber 1286275-72-6 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,2,8,6,2,7 and 5 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 1286275-72:
(9*1)+(8*2)+(7*8)+(6*6)+(5*2)+(4*7)+(3*5)+(2*7)+(1*2)=186
186 % 10 = 6
So 1286275-72-6 is a valid CAS Registry Number.

1286275-72-6Relevant articles and documents

Substituted 2-thioxothiazolidin-4-one derivatives showed protective effects against diabetic cataract via inhibition of aldose reductase

Huang, Wanrong,Zhang, Yue,Liang, Xu,Yang, Lichun

, (2020)

In an effort to develop a new class of potent aldose reductase inhibitors against diabetic cataracts, a series of novel 2-thioxothiazolidine-4-one derivatives was synthesized in excellent yields via a facile synthetic route. These compounds were tested against aldehyde (ALR1) and aldose reductase (ALR2) enzymes, where they showed considerable inhibitory activity. Among the tested derivatives, compound 6e showed selective and excellent inhibition of ALR2 over ALR1. The experimental diabetes was induced by the intraperitoneal administration of streptozotocin in male Wistar rats. Compound 6e showed positive modulation of body weight, blood glucose, and blood insulin levels in diabetic rats. Compound 6e also showed ALR2 inhibition as evidenced by Western blot analysis in lens homogenates of Wistar rats having cataract. The docking study of 6e was also performed inside the active site of ALR2 to enumerate the key contacts for inhibitory activity.

Piperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation

Hammill, Jared T.,Scott, Daniel C.,Min, Jaeki,Connelly, Michele C.,Holbrook, Gloria,Zhu, Fangyi,Matheny, Amy,Yang, Lei,Singh, Bhuvanesh,Schulman, Brenda A.,Guy, R. Kiplin

supporting information, p. 2680 - 2693 (2018/04/23)

We previously discovered and validated a class of piperidinyl ureas that regulate defective in cullin neddylation 1 (DCN1)-dependent neddylation of cullins. Here, we report preliminary structure-activity relationship studies aimed at advancing our high-throughput screen hit into a tractable tool compound for dissecting the effects of acute DCN1-UBE2M inhibition on the NEDD8/cullin pathway. Structure-enabled optimization led to a 100-fold increase in biochemical potency and modestly increased solubility and permeability as compared to our initial hit. The optimized compounds inhibit the DCN1-UBE2M protein-protein interaction in our TR-FRET binding assay and inhibit cullin neddylation in our pulse-chase NEDD8 transfer assay. The optimized compounds bind to DCN1 and selectively reduce steady-state levels of neddylated CUL1 and CUL3 in a squamous cell carcinoma cell line. Ultimately, we anticipate that these studies will identify early lead compounds for clinical development for the treatment of lung squamous cell carcinomas and other cancers.

Development of cholinesterase inhibitors using 1-benzyl piperidin-4-yl (α)-lipoic amide molecules

Lee, Seung-Hwan,Kim, Beom-Cheol,Kim, Jae-Kwan,Lee, Hye Sook,Shon, Min Young,Park, Jeong Ho

, p. 1681 - 1686 (2014/07/07)

A series of hybrid molecules between (α)-lipoic acid (ALA) and 4-amino-1-benzyl piperidines were synthesized and their in vitro cholinesterase (acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)) inhibitory activities were evaluated. Even thoug

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