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27646-28-2

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27646-28-2 Usage

General Description

(S)-1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethan-1-ol is a chemical compound with the molecular formula C11H10Cl2N2O. It is a chiral compound, meaning it has a non-superimposable mirror image, and it has two enantiomers (S)- and (R)-. (S)-1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethan-1-ol is a derivative of imidazole and is commonly used as an antifungal medication. It works by disrupting the cell membrane of fungi, leading to their death. It is often used to treat fungal infections such as athlete's foot, ringworm, and jock itch. Additionally, it has been studied for its potential use in cancer treatment due to its ability to inhibit the growth of cancer cells.

Check Digit Verification of cas no

The CAS Registry Mumber 27646-28-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,7,6,4 and 6 respectively; the second part has 2 digits, 2 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 27646-28:
(7*2)+(6*7)+(5*6)+(4*4)+(3*6)+(2*2)+(1*8)=132
132 % 10 = 2
So 27646-28-2 is a valid CAS Registry Number.

27646-28-2Relevant articles and documents

Sterol 14α-Demethylase Structure-Based Design of VNI ((R)- N-(1-(2,4-Dichlorophenyl)-2-(1 H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)benzamide)) Derivatives to Target Fungal Infections: Synthesis, Biological Evaluation, and Crystallographic Analysis

Friggeri, Laura,Hargrove, Tatiana Y.,Wawrzak, Zdzislaw,Blobaum, Anna L.,Rachakonda, Girish,Lindsley, Craig W.,Villalta, Fernando,Nes, W. David,Botta, Maurizio,Guengerich, F. Peter,Lepesheva, Galina I.

, p. 5679 - 5691 (2018/06/22)

Because of the increase in the number of immunocompromised patients, the incidence of invasive fungal infections is growing, but the treatment efficiency remains unacceptably low. The most potent clinical systemic antifungals (azoles) are the derivatives of two scaffolds: ketoconazole and fluconazole. Being the safest antifungal drugs, they still have shortcomings, mainly because of pharmacokinetics and resistance. Here, we report the successful use of the target fungal enzyme, sterol 14α-demethylase (CYP51), for structure-based design of novel antifungal drug candidates by minor modifications of VNI [(R)-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)benzamide)], an inhibitor of protozoan CYP51 that cures Chagas disease. The synthesis of fungi-oriented VNI derivatives, analysis of their potencies to inhibit CYP51s from two major fungal pathogens (Aspergillus fumigatus and Candida albicans), microsomal stability, effects in fungal cells, and structural characterization of A. fumigatus CYP51 in complexes with the most potent compound are described, offering a new antifungal drug scaffold and outlining directions for its further optimization.

A convergent, scalable and stereoselective synthesis of azole CYP51 inhibitors

Lepesheva, Galina,Christov, Plamen,Sulikowski, Gary A.,Kim, Kwangho

supporting information, p. 4248 - 4250 (2017/10/12)

The study and development of azole-based CYP51 inhibitors is an active area of research across disciplines of biochemistry, pharmacology and infectious disease. Support of in vitro and in vivo studies require the development of robust asymmetric routes to single enantiomer products of this class of compounds. Herein, we describe a scalable and enantioselective synthesis to VNI and VFV, the two potent inhibitors of protozoan sterol 14α-demethylase (CYP51) that are currently under consideration for clinical trials for Chagas disease. A key transformation is the Jacobsen Hydrolytic Kinetic Resolution (HKR) reaction. The utility of the synthetic route is illustrated by the preparation of >25 g quantities of single enantiomers of VNI and VFV.

Structural basis for rational design of inhibitors targeting Trypanosoma cruzi Sterol 14α-demethylase: Two regions of the enzyme molecule potentiate its inhibition

Friggeri, Laura,Hargrove, Tatiana Y.,Rachakonda, Girish,Williams, Amanda D.,Wawrzak, Zdzislaw,Di Santo, Roberto,De Vita, Daniela,Waterman, Michael R.,Tortorella, Silvano,Villalta, Fernando,Lepesheva, Galina I.

, p. 6704 - 6717 (2014/09/29)

Chagas disease, which was once thought to be confined to endemic regions of Latin America, has now gone global, becoming a new worldwide challenge with no cure available. The disease is caused by the protozoan parasite Trypanosoma cruzi, which depends on the production of endogenous sterols, and therefore can be blocked by sterol 14α-demethylase (CYP51) inhibitors. Here we explore the spectral binding parameters, inhibitory effects on T. cruzi CYP51 activity, and antiparasitic potencies of a new set of β-phenyl imidazoles. Comparative structural characterization of the T. cruzi CYP51 complexes with the three most potent inhibitors reveals two opposite binding modes of the compounds ((R)-6, EC50 = 1.2 nM, vs (S)-2/(S)-3, EC50 = 1.0/5.5 nM) and suggests the entrance into the CYP51 substrate access channel and the heme propionate-supporting ceiling of the binding cavity as two distinct areas of the protein that enhance molecular recognition and therefore could be used for the development of more effective antiparasitic drugs.

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