171778-06-6 Usage
General Description
3-(9-Fluorenylmethyloxycarbonyl)amino-3-(2-nitrophenyl)propionic acid is a compound with potential applications in the field of biochemistry and pharmaceuticals. It contains a fluorenylmethyloxycarbonyl (Fmoc) protecting group, which is commonly used in peptide synthesis to protect the amino group of amino acids. The presence of the 2-nitrophenyl group in the molecule gives it potential photophysical and photochemical properties, making it suitable for use in photodynamic therapy or as a fluorophore in bioimaging applications. In addition, the propionic acid moiety in the molecule could also contribute to its potential use as a nonsteroidal anti-inflammatory drug. Overall, this compound's unique structure and functional groups make it an interesting candidate for further research and potential applications in various fields.
Check Digit Verification of cas no
The CAS Registry Mumber 171778-06-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,7,1,7,7 and 8 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 171778-06:
(8*1)+(7*7)+(6*1)+(5*7)+(4*7)+(3*8)+(2*0)+(1*6)=156
156 % 10 = 6
So 171778-06-6 is a valid CAS Registry Number.
InChI:InChI=1/C24H20N2O6/c27-23(28)13-21(19-11-5-6-12-22(19)26(30)31)25-24(29)32-14-20-17-9-3-1-7-15(17)16-8-2-4-10-18(16)20/h1-12,20-21H,13-14H2,(H,25,29)(H,27,28)
171778-06-6Relevant articles and documents
Light-mediated liberation of enzymatic activity: Small molecule caged protein equivalents
Li, Haishan,Hah, Jung-Mi,Lawrence, David S.
supporting information; experimental part, p. 10474 - 10475 (2009/02/05)
Light-activatable ( caged ) proteins have been used to correlate, with exquisite temporal and spatial control, intracellular biochemical action with global cellular behavior. However, the chemical or genetic construction of caged proteins is nontrivial, with subsequent laborious introduction into living cells, potentially problematic competition with natural endogenous counterparts, and challenging intracellular incorporation at levels equivalent to the natural enzymes. We describe the design, synthesis, and characterization of small molecular equivalents of a caged Src kinase. These compounds are easy to prepare and function by inhibiting the action of the natural unmodified enzyme. Copyright
