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(3S)-3-(N-benzyloxycarbonyl)amino-2-keto-4-phenylbutyryl-L-prolyl-tert-butyl amide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

141197-75-3

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141197-75-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 141197-75-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,1,1,9 and 7 respectively; the second part has 2 digits, 7 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 141197-75:
(8*1)+(7*4)+(6*1)+(5*1)+(4*9)+(3*7)+(2*7)+(1*5)=123
123 % 10 = 3
So 141197-75-3 is a valid CAS Registry Number.

141197-75-3Downstream Products

141197-75-3Relevant academic research and scientific papers

HIV protease inhibitors

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Page/Page column 25, (2010/02/11)

Combinatorial libraries of HIV and FIV protease inhibitors are characterized by alpha-keto amide or hydroxyethylamine core structures flanked by on one side by substituted pyrrolidines, piperidines, or azasugars and on the other side by phenylalanine, tyrosine, or substituted tyrosines. The libraries are synthesized via a one step coupling reaction. Highly efficacious drug candidates are identified by screening the libraries for binding and inhibitory activity against both HIV and FIV protease. Drug candidates displaying clinically useful activity against both HIV and FIV protease are identified as being potentially resistive against a loss of inhibitory activity due to development of resistant strains of HIV.

Development of a new type of protease inhibitors, efficacious against FIV and HIV variants

Lee, Taekyu,Le, Van-Duc,Lim, Dongyeol,Lin, Ying-Chuan,Morris, Garrett M.,Wong, Andrew L.,Olson, Arthur J.,Elder, John H.,Wong, Chi-Huey

, p. 1145 - 1155 (2007/10/03)

Based on the structural analysis of FIV protease and drug-resistant HIV proteases and molecular modeling, a new type of inhibitors with a small P3 residue has been developed. These inhibitors are effective against HIV and its drug-resistant mutants, as well as SIV and FIV. Modification of existing HIV protease inhibitors by reducing the size of the P3 residue has the same effect. This finding provides a new strategy for the development of HIV protease inhibitors effective against the wild-type and drug-resistant mutants. It further supports the use of FIV protease as a useful model for drug-resistant HIV proteases, which often have a more constricted binding region for the P3 group or the combined P3 and P1 groups.

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