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6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one is a chemical compound characterized by its unique molecular structure, which features a pteridine core with phenyl and sulfanylidene groups attached. "6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one has potential applications in various fields due to its distinct chemical properties and interactions with other molecules.

14892-97-8

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14892-97-8 Usage

Uses

Used in Pharmaceutical Industry:
6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one is used as a pharmaceutical candidate for its potential therapeutic effects. The compound's unique structure allows it to interact with specific biological targets, making it a promising candidate for the development of new drugs.
Used in Chemical Research:
6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one is used as a research tool in the field of chemistry to study its properties and potential applications. Its unique structure and reactivity make it an interesting subject for further investigation and development.
Used in CRISPR/Cas9-mediated Editing:
6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one is used as a non-homologous end joining (NHEJ) modulator to study its effect on CRISPR/Cas9-mediated editing. By modulating the NHEJ process, "6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one can potentially enhance the efficiency and accuracy of CRISPR/Cas9 gene editing techniques.

Biological Activity

scr7 pyrazine is an inhibitor of dna ligase iv [1].dna ligase iv is involved in sealing of double-strand breaks (dsbs) during nonhomologous end-joining (nhej). dsbs have been considered as one of the most lethal types of dna damage within cells. unrepaired dsbs may lead to chromosomal rearrangements such as translocations and deletions, resulting in oncogenic transformations or cell death. in higher eukaryotes, nhej is one of the primary mechanisms of dsb repair and is active throughout the cell cycle. nhej plays a major role in providing resistance to cancer cells to these radio- and chemotherapy agents [1].scr7 blocked ligase iv-mediated joining by interfering with its dna binding in cell-free repair system. scr7 inhibited nhej in a ligase iv-dependent manner within cells, and activated the intrinsic apoptotic pathway. scr7 dose-dependent decreased cell proliferation in mcf7, a549, and hela cells with an ic50 of 40, 34, and 44 μm, respectively. in t47d, a2780, and ht1080 cells, the ic50 values were 8.5, 120, and 10 μm, respectively [1].scr7 treatment (10 mg/kg, six doses) significantly reduced breast adenocarcinoma-induced tumor and impeded tumor progression in mouse models in mouse models. coadministered of scr7 with dsb-inducing therapeutic modalities significantly enhanced their sensitivity.

Biochem/physiol Actions

SCR7 pyrazine is reported to be an inhibitor of non-homologous end joining (NHEJ) and has been shown to enhance the efficiency of CRISPR-Cas9 genome editing. The effect of SCR7 pyrazine on the efficiency and targeting precision of CRISPR applications has been shown to be cell type specific and context dependent. SCR7 pyrazine is a product of spontaneous cyclization of SCR7, first reported by Srivastava, M., et al.

references

[1] srivastava m, nambiar m, sharma s, et al. an inhibitor of nonhomologous end-joining abrogates double-strand break repair and impedes cancer progression[j]. cell, 2012, 151(7): 1474-1487.

Check Digit Verification of cas no

The CAS Registry Mumber 14892-97-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,8,9 and 2 respectively; the second part has 2 digits, 9 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 14892-97:
(7*1)+(6*4)+(5*8)+(4*9)+(3*2)+(2*9)+(1*7)=138
138 % 10 = 8
So 14892-97-8 is a valid CAS Registry Number.

14892-97-8 Well-known Company Product Price

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  • Sigma

  • (SML1546)  SCR7 pyrazine  ≥98% (HPLC)

  • 14892-97-8

  • SML1546-5MG

  • 983.97CNY

  • Detail
  • Sigma

  • (SML1546)  SCR7 pyrazine  ≥98% (HPLC)

  • 14892-97-8

  • SML1546-25MG

  • 3,970.98CNY

  • Detail

14892-97-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name 6,7-diphenyl-2-sulfanylidene-1H-pteridin-4-one

1.2 Other means of identification

Product number -
Other names 4-Oxo-6,7-diphenyl-2-thioxotetrahydropteridin

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:14892-97-8 SDS

14892-97-8Relevant academic research and scientific papers

Synthesis and structure determination of SCR7, a DNA ligase inhibitor

Greco, George E.,Conrad, Zane A.,Johnston, Alycia M.,Li, Qingyao,Tomkinson, Alan E.

, p. 3204 - 3207 (2016)

In contrast to a published report, reaction of 4,5-diamino-6-hydroxy-2-mercaptopyrimidine with 2?equiv of aromatic aldehydes produces a mixture of 6,7-diaryl-2-thioxopteridine-4-one and 6,7-diaryl-2-thioxo-7,8-dihydropteridine-4-one rather than a diimine. These compounds represent the correct structure for SCR7, a substance reported to be an inhibitor of nonhomologous end-joining, a DNA repair pathway. The dihydropteridine can be isolated as a minor product, and it can be oxidized to the pteridine.

Autocyclized and oxidized forms of SCR7 induce cancer cell death by inhibiting nonhomologous DNA end joining in a Ligase IV dependent manner

Vartak, Supriya V.,Swarup, Hassan A.,Gopalakrishnan, Vidya,Gopinatha, Vindya K.,Ropars, Virginie,Nambiar, Mridula,John, Franklin,Kothanahally, Sharath Kumar S.,Kumari, Rupa,Kumari, Nitu,Ray, Ujjayinee,Radha, Gudapureddy,Dinesh, Depina,Pandey, Monica,Ananda, Hanumappa,Karki, Subhas S.,Srivastava, Mrinal,Charbonnier, Jean Baptiste,Choudhary, Bibha,Mantelingu, Kempegowda,Raghavan, Sathees C.

, p. 3959 - 3976 (2018)

Nonhomologous DNA end joining (NHEJ) is the major DNA double-strand break (DSB) repair pathway in mammals. Previously, we have described a small molecule inhibitor, SCR7, which can inhibit NHEJ in a Ligase IV-dependent manner. Administration of SCR7 within the cells resulted in the accumulation of DNA breaks, cell death, and inhibition of tumor growth in mice. In the present study, we report that parental SCR7, which is unstable, can be autocyclized into a stable form. Both parental SCR7 and cyclized SCR7 possess the same molecular weight (334.09) and molecular formula (C18H14N4OS), whereas its oxidized form, SCR7-pyrazine, possesses a different molecular formula (C18H12N4OS), molecular weight (332.07), and structure. While cyclized form of SCR7 showed robust inhibition of NHEJ in vitro, both forms exhibited efficient cytotoxicity. Cyclized and oxidized forms of SCR7 inhibited DNA end joining catalyzed by Ligase IV, whereas their impact was minimal on Ligase III, Ligase I, and T4 DNA Ligase-mediated joining. Importantly, both forms inhibited V(D)J recombination, although the effect was more pronounced for SCR7-cyclized. Both forms blocked NHEJ in a Ligase IV-dependent manner leading to the accumulation of DSBs within the cells. Although cytotoxicity due to SCR7-cyclized was Ligase IV specific, the pyrazine form exhibited nonspecific cytotoxicity at higher concentrations in Ligase IV-null cells. Finally, we demonstrate that both forms can potentiate the effect of radiation. Thus, we report that cyclized and oxidized forms of SCR7 can inhibit NHEJ in a Ligase IV-dependent manner, although SCR7-pyrazine is less specific to Ligase IV inside the cell.

NOVEL NUCLEIC ACID MODIFIERS

-

Sheet 7, (2019/07/20)

The present inventions generally relate to site-specific delivery of nucleic acid modifiers and includes novel DNA-binding proteins and effectors that can be rapidly programmed to make site-specific DNA modifications. The present inventions also provide a synthetic all-in-one genome editor (SAGE) systems comprising designer DNA sequence readers and a set of small molecules that induce double-strand breaks, enhance cellular permeability, inhibit NHEJ and activate HDR, as well as methods of using and delivering such systems.

Discovery of HIV-1 integrase inhibitors: Pharmacophore mapping, virtual screening, molecular docking, synthesis, and biological evaluation

Bhatt, Hardik,Patel, Paresh,Pannecouque, Christophe

, p. 154 - 166 (2014/02/14)

HIV-1 integrase enzyme plays an important role in the life cycle of HIV and responsible for integration of virus into human genome. Here, both computational and synthetic approaches were used to design and synthesize newer HIV-1 integrase inhibitors. Pharmacophore mapping was performed on 20 chemically diverse molecules using DISCOtech, and refinement was carried out using GASP. Ten pharmacophore models were generated, and model 2, containing four features including two donor sites, one acceptor atom, and one hydrophobic region, was considered the best model as it has the highest fitness score. It was used as a query in NCI and Maybridge databases. Molecules having more than 99% Q fit value were used to design 30 molecules bearing pteridine ring and were docked on co-crystal structure of HIV-1 integrase enzyme. Among these, six molecules, showing good docking score compared with the reference standards, were synthesized by conventional as well as microwave-assisted methods. All compounds were characterized by physical and spectral data and evaluated for in vitro anti-HIV activity against the replication of HIV-1 (IIIB) in MT-4 cells. The used approach of molecular docking and anti-HIV activity data of designed molecules will provide significant insights to discover novel HIV-1 Integrase Inhibitors. Computer-aided drug design approaches like pharmacophore mapping, virtual screening, and molecular docking were used to design novel compounds bearing pteridine ring system. Designed compounds were synthesized by conventional and microwave-irradiated methods showing advantage of MWI method. All synthesized compounds were evaluated as HTV-1 integrase inhibitors and further explored to discover novel HIV-I integrase inhibitors.

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