1460-46-4 Usage
General Description
α-Cyclopropyl-α-hydroxybenzeneacetic acid, also known as carprofen, is a non-steroidal anti-inflammatory drug (NSAID) used in veterinary medicine for the treatment of pain and inflammation in dogs and horses. It belongs to the propionic acid class of NSAIDs and works by blocking the production of prostaglandins, which are chemicals that cause pain and inflammation. Carprofen is commonly used to manage arthritis and postoperative pain in animals. It is available in various forms, including tablets, caplets, and injectable solutions, and is generally well tolerated with few side effects when used at the prescribed dosage. However, like all NSAIDs, carprofen can have adverse effects on the gastrointestinal, renal, and hepatic systems and should be used with caution, especially in animals with pre-existing medical conditions.
Check Digit Verification of cas no
The CAS Registry Mumber 1460-46-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,4,6 and 0 respectively; the second part has 2 digits, 4 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1460-46:
(6*1)+(5*4)+(4*6)+(3*0)+(2*4)+(1*6)=64
64 % 10 = 4
So 1460-46-4 is a valid CAS Registry Number.
InChI:InChI=1/C11H12O3/c12-10(13)11(14,9-6-7-9)8-4-2-1-3-5-8/h1-5,9,14H,6-7H2,(H,12,13)
1460-46-4Relevant articles and documents
Identification of Novel Fragments Binding to the PDZ1-2 Domain of PSD-95
Zang, Jie,Ye, Fei,Solbak, Sara M. ?.,H?j, Lars J.,Zhang, Mingjie,Bach, Anders
supporting information, p. 949 - 954 (2020/12/31)
Inhibition of PSD-95 has emerged as a promising strategy for the treatment of ischemic stroke, as shown with peptide-based compounds that target the PDZ domains of PSD-95. In contrast, developing potent and drug-like small molecules against the PSD-95 PDZ domains has so far been unsuccessful. Here, we explore the druggability of the PSD-95 PDZ1-2 domain and use fragment screening to investigate if this protein is prone to binding small molecules. We screened 2500 fragments by fluorescence polarization (FP) and validated the hits by surface plasmon resonance (SPR), including an inhibition counter-test, and found four promising fragments. Three ligand efficient fragments were shown by 1H,15N HSQC NMR to bind in the small hydrophobic P0 pockets of PDZ1-2, and one of them underwent structure-activity relationship (SAR) studies. Overall, we demonstrate that fragment screening can successfully be applied to PDZ1-2 of PSD-95 and disclose novel fragments that can serve as starting points for optimization towards small-molecule PDZ domain inhibitors.
