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2-methyl-4,4-diphenylbuta-2,3-dienoic acid is a chemical compound with the molecular formula C18H16O2. It is an organic molecule characterized by a buta-2,3-dienoic acid structure, which features a conjugated diene system with a double bond at the 2nd and 3rd carbon atoms. The molecule also contains a methyl group attached to the 2nd carbon and two phenyl rings bonded to the 4th carbon. 2-methyl-4,4-diphenylbuta-2,3-dienoic acid is known for its potential applications in the synthesis of various pharmaceuticals and other organic compounds due to its unique structure and reactivity. It is an example of a substituted butadiene derivative, which can participate in various chemical reactions, such as Diels-Alder cycloadditions, due to its conjugated diene system.

6002-06-8

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6002-06-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 6002-06-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 6,0,0 and 2 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 6002-06:
(6*6)+(5*0)+(4*0)+(3*2)+(2*0)+(1*6)=48
48 % 10 = 8
So 6002-06-8 is a valid CAS Registry Number.

6002-06-8Downstream Products

6002-06-8Relevant academic research and scientific papers

Possible involvement of radical intermediates in the inhibition of cysteine proteases by allenyl esters and amides

Takeuchi, Yoshio,Fujiwara, Tomoya,Shimone, Yoshihito,Miyataka, Hideki,Satoh, Toshio,Kirk, Kenneth L.,Hori, Hitoshi

scheme or table, p. 6202 - 6205 (2009/08/07)

In order to investigate crystallographically the mechanism of inhibition of cysteine protease by α-methyl-γ,γ-diphenylallenecarboxylic acid ethyl ester 3, a cysteine protease inhibitor having in vivo stability, we synthesized N-(α-methyl-γ,γ-diphenylallenecarbonyl)-l-phenylalanin e ethyl ester 4. Reaction of 4 with thiophenol, the SH group of which has similar pKa value to that of cysteine protease, produced oxygen-mediated radical adducts 6 and 7 in ambient air but did not proceed under oxygen-free conditions. Catalytic activities of two thiol enzymes including cathepsin B were also lowered in the absence of oxygen. These results suggest that cysteine protease can act through an oxygen-dependent radical mechanism.

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