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270088-04-5

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270088-04-5 Usage

Uses

7-Ethynylcoumarin is a selective inhibitors of human cytochrome P450s 1A1 and 1A2.

Check Digit Verification of cas no

The CAS Registry Mumber 270088-04-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,7,0,0,8 and 8 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 270088-04:
(8*2)+(7*7)+(6*0)+(5*0)+(4*8)+(3*8)+(2*0)+(1*4)=125
125 % 10 = 5
So 270088-04-5 is a valid CAS Registry Number.

270088-04-5Relevant articles and documents

Synthesis and antimycobacterial activity of 1-(β-D-Ribofuranosyl)-4-coumarinyloxymethyl- / -coumarinyl-1,2,3-triazole

Srivastava, Smriti,Bimal, Devla,Bohra, Kapil,Singh, Balram,Ponnan, Prija,Jain, Ruchi,Varma-Basil, Mandira,Maity, Jyotirmoy,Thirumal,Prasad, Ashok K.

, p. 268 - 281 (2018/03/21)

A series of β-D-ribofuranosyl coumarinyl-1,2,3-triazoles have been synthesized by Cu-catalyzed cycloaddition reaction between azidosugar and 7-O-/7-alkynylated coumarins in 62–70% overall yields. The in vitro antimycobacterial activity evaluation of the s

7-ethynylcoumarins: Selective inhibitors of human cytochrome P450s 1A1 and 1A2

Liu, Jiawang,Nguyen, Thong T.,Dupart, Patrick S.,Sridhar, Jayalakshmi,Zhang, Xiaoyi,Zhu, Naijue,Stevens, Cheryl L. Klein,Foroozesh, Maryam

, p. 1047 - 1057 (2012/08/13)

To discover new selective mechanism-based P450 inhibitors, eight 7-ethynylcoumarin derivatives were prepared through a facile two-step synthetic route. Cytochrome P450 activity assays indicated that introduction of functional groups in the backbone of coumarin could enhance the inhibition activities toward P450s 1A1 and 1A2, providing good selectivity against P450s 2A6 and 2B1. The most potent product 7-ethynyl-3,4,8-trimethylcoumarin (7ETMC) showed IC 50 values of 0.46 μM and 0.50 μM for P450s 1A1 and 1A2 in the first six minutes, respectively, and did not show any inhibition activity for P450s 2A6 and 2B1 even at the dose of 50 μM. All of the inhibitors except 7-ethynyl-3-methyl-4-phenylcoumarin (7E3M4PC) showed mechanism-based inhibition of P450s 1A1 and 1A2. In order to explain this mechanistic difference in inhibitory activities, X-ray crystallography data were used to study the difference in conformation between 7E3M4PC and the other compounds studied. Docking simulations indicated that the binding orientations and affinities resulted in different behaviors of the inhibitors on P450 1A2. Specifically, 7E3M4PC with its two-plane structure fits into the P450 1A2's active site cavity with an orientation leading to no reactive binding, causing it to act as a competitive inhibitor.

Mechanism-based inactivation of cytochrome P450 2B1 by 7- ethynylcoumarin: Verification of apo-P450 adduction by electrospray ion trap mass spectrometry

Regal, Kelly A.,Schrag, Michael L.,Kent, Ute M.,Wienkers, Larry C.,Hollenberg, Paul F.

, p. 262 - 270 (2007/10/03)

7-Ethynylcoumarin was synthesized as a potential mechanism-based inhibitor, and it was found to be an effective inactivator of 7-ethoxy-4- (trifluoromethyl)coumarin (7EFC) O-deethylation catalyzed by purified, reconstituted P450 2B1. In contrast, 7-ethynylcoumarin demonstrated minimal inactivation of P450 2A6-mediated 7-hydroxycoumarin formation. The inactivation of P450 2B1 demonstrated pseudo-first-order kinetics and was NADPH- and inhibitor-dependent. The maximal rate constant for the inactivation of 2B1 was 0.39 min-1 at 30 °C, and thus, the time required to inactivate 50% of the P450 2B1 that was present (t( 1/2 )) was 1.8 min. The estimated concentration which led to half-maximal inactivation (K(I)) was 25 μM. No protection from inactivation was seen in the presence of nucleophiles (glutathione and sodium cyanide), an iron chelator (deferroxamine), or superoxide dismutase and catalase. Addition of the substrate (7EFC) protected P450 2B1 from inactivation, in a concentration-dependent manner. The partition ratio for P450 2B1 was 25; i.e., the number of metabolic events was 25-fold higher than the number of inactivating events. Incubations of 7- ethynylcoumarin with P450 2B1 for 10 min resulted in an 80% loss in enzymatic activity, while 90% of the ability to form a reduced-CO complex remained. This activity loss was not recovered following dialysis, indicative of irreversible inactivation. Covalent attachment of the entire inhibitor and oxygen to apo-P450 2B1, in a 1:1 ratio, was shown via electrospray ion trap mass spectrometry. This method also verified the absence of modification to the heme or the cytochrome P450 reductase. Taken together, the characterization of the inhibition seen with P450 2B1 and 7-ethynylcoumarin was consistent with all of the criteria required to distinguish a mechanism- based inactivator. In addition, electrospray ion trap mass spectrometry has the potential to be applied to protein adducts above and beyond those associated with the mechanism-based inactivation of cytochrome P450s.

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