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{1-[5-(1-benzyloxycarbonylamino-3-methyl-butyl)-2,2-dimethyl-[1,3]dioxolan-4-yl]-3-methyl-butyl}-carbamic acid benzyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

142285-44-7

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142285-44-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 142285-44-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,2,2,8 and 5 respectively; the second part has 2 digits, 4 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 142285-44:
(8*1)+(7*4)+(6*2)+(5*2)+(4*8)+(3*5)+(2*4)+(1*4)=117
117 % 10 = 7
So 142285-44-7 is a valid CAS Registry Number.

142285-44-7Relevant academic research and scientific papers

Expedient solid-phase synthesis of both symmetric and asymmetric diol libraries targeting aspartic proteases

Shi, Haibin,Liu, Kai,Leong, Wendy W.Y.,Yao, Shao Q.

supporting information; experimental part, p. 3945 - 3948 (2010/03/30)

C2-symmetric diols have been shown to be highly potent against HIV-1 protease (PR). However, gaining access to these compounds has been hampered by the need of multistep solution-phase reactions which are often tedious and inefficient. In this Letter, we have disclosed a solid-phase strategy for rapid preparation of small molecule-based, symmetric and asymmetric diols as potential HIV-1 protease inhibitors. Upon biological screening, we found one of them, SYM-5, to be a potent and selective inhibitor (Ki = 400 nM) against HIV-1 protease.

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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