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L-N-(benzyloxycarbonyl)-O-<(1,1-dimethylethyl)dimethylsilyloxy>tyrosine methyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

226211-52-5

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226211-52-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 226211-52-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,2,6,2,1 and 1 respectively; the second part has 2 digits, 5 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 226211-52:
(8*2)+(7*2)+(6*6)+(5*2)+(4*1)+(3*1)+(2*5)+(1*2)=95
95 % 10 = 5
So 226211-52-5 is a valid CAS Registry Number.

226211-52-5Relevant academic research and scientific papers

Modular construction of quaternary hemiaminal-based inhibitor candidates and their in cellulo assessment with HIV-1 protease

Gros, Guillaume,Martinez, Lorena,Gimenez, Anna Servat,Adler, Paula,Maurin, Philippe,Wolkowicz, Roland,Falson, Pierre,Hasserodt, Jens

, p. 5407 - 5413 (2013/09/02)

Non-peptidomimetic drug-like protease inhibitors have potential for circumventing drug resistance. We developed a much-improved synthetic route to our previously reported inhibitor candidate displaying an unusual quaternized hemi-aminal. This functional group forms from a linear precursor upon passage into physiological media. Seven variants were prepared and tested in cellulo with our HIV-1 fusion-protein technology that result in an eGFP-based fluorescent readout. Three candidates showed inhibition potency above 20 μM and toxicity at higher concentrations, making them attractive targets for further refinement. Importantly, our class of original inhibitor candidates is not recognized by two major multidrug resistance pumps, quite in contrast to most clinically applied HIV-1 protease inhibitors.

Synthesis of a series of stromelysin-selective thiadiazole urea matrix metalloproteinase inhibitors

Jacobsen, E. Jon,Mitchell, Mark A.,Hendges, Susan K.,Belonga, Kenneth L.,Skaletzky, Louis L.,Stelzer, Lindsay S.,Lindberg, Thomas J.,Fritzen, Edward L.,Schostarez, Heinrich J.,O'Sullivan, Theresa J.,Maggiora, Linda L.,Stuchly, Christopher W.,Laborde, Alice L.,Kubicek, Marc F.,Poorman, Roger A.,Beck, Joan M.,Miller, Henry R.,Petzold, Gary L.,Scott, Pam S.,Truesdell, Scott E.,Wallace, Tanya L.,Wilks, John W.,Fisher, Christopher,Goodman, Linda V.,Kaytes, Paul S.,Ledbetter, Stephen R.,Powers, Elaine A.,Vogeli, Gabriel,Mott, John E.,Trepod, Catherine M.,Staples, Douglas J.,Baldwin, Eric T.,Finzel, Barry C.

, p. 1525 - 1536 (2007/10/03)

The synthesis and enzyme inhibition data for a series of thiadiazole urea matrix metalloproteinase (MMP) inhibitors are described. A broad screening effort was utilized to identify several thiadiazoles which were weak inhibitors of stromelysin. Optimization of the thiadiazole leads to include an α-amino acid side chain with variable terminal amide substituents provided a series of ureas which were moderately effective stromelysin inhibitors, with K(i)'s between 0.3 and 1.0 μM. The most effective analogues utilized an L-phenylalanine as the amino acid component. In particular, unsubstituted 46 had a K(i) of 710 nM, while the p-fluoro analogue 52 displayed increased potency (100 nM). Stromelysin inhibition was further improved using a pentafluorophenylalanine substituent which resulted in 70, a 14 nM inhibitor. While gelatinase inhibition was generally poor, the use of 1-(2-pyridyl)piperazine as the amide component usually provided for enhanced activity, with 71 inhibiting gelatinase with a K(i) of 770 nM. The combination of this heterocycle with a p-fluorophenylalanine substituent provided the only analogue, 69, with collagenase activity (13 μM). The SAR for analogues described within this series can be rationalized through consideration of the X-ray structure recently attained for 70 complexed to stromelysin. Uniquely, this structure showed the inhibitor to be completely orientated on the left side of the enzyme cleft. These results suggest that thiadiazole urea heterocycles which incorporate a substituted phenylalanine can provide selective inhibitors of stromelysin. Careful selection of the amide substituent can also provide for analogues with modest gelatinase inhibition.

The total synthesis of the diepoxycyclohexanone antibiotic aranorosin and novel synthetic analogues

McKillop, Alexander,McLaren, Lee,Taylor, Richard J. K.,Watson, Robert J.,Lewis, Norman J.

, p. 1385 - 1393 (2007/10/03)

A short synthesis of the novel antibiotic aranorosin in chiral form is described which employs (i) a novel hypervalent iodine-mediated oxidative hydroxylation of a tyrosinal derivative and (ii) a stereocontrolled cis-bisepoxidation in the key steps. A similar procedure was employed to prepare 6′-epiaranorosin, and hence establish the stereochemistry of the natural compound, and to prepare novel aranorosin analogues. An organometallic route is described which gives desamidoaranorosin.

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