18205-99-7Relevant articles and documents
Redox regulation of protein tyrosine phosphatase 1B (PTP1B): A biomimetic study on the unexpected formation of a sulfenyl amide intermediate
Sarma, Bani Kanta,Mugesh, Govindasamy
, p. 8872 - 8881 (2007)
The effect of steric and electronic environments around the sulfur and nitrogen atoms and the role of nonbonded S...O/N interactions on the cyclization reactions of amide substituted benzene sulfenic acids are described. The reaction profiles and the role
Electrochemical synthesis for benzisothiazol-3(2H)-ones by dehydrogenative N[sbnd]S bond formation
Chen, Junmin,Sheng, Shouri,Xiong, Zhiqiang,Zhong, Qihao
supporting information, (2021/08/26)
Herein, we report an electrochemical method for the synthesis of benzisothiazol-3(2H)-ones from 2-mercaptobenzamides. The electrochemical reaction proceeds through intramolecular N[sbnd]H/S[sbnd]H coupling cyclization reaction by generating H2 as the nonhazardous side product. Moreover, the developed procedure is highly advantageous due to its short reaction time, mild conditions and wide substrate scope without the employment of metal catalyst and exogenous-oxidant.2009 Elsevier Ltd. All rights reserved.
Electron paramagnetic resonance spectroscopy as a probe of hydrogen bonding in heme-Thiolate proteins
Dent, Matthew R.,Milbauer, Michael W.,Hunt, Andrew P.,Aristov, Michael M.,Guzei, Ilia A.,Lehnert, Nicolai,Burstyn, Judith N.
, p. 16011 - 16027 (2019/11/28)
Despite utilizing a common cofactor binding motif, hemoproteins bearing a cysteine-derived thiolate ligand (heme-Thiolate proteins) are involved in a diverse array of biological processes ranging from drug metabolism to transcriptional regulation. Though the origin of heme-Thiolate functional divergence is not well understood, growing evidence suggests that the hydrogen bonding (H-bonding) environment surrounding the Fe-coordinating thiolate influences protein function. Outside of X-ray crystallography, few methods exist to characterize these critical H-bonding interactions. Electron paramagnetic resonance (EPR) spectra of heme-Thiolate proteins bearing a six-coordinate, Fe(III) heme exhibit uniquely narrow low-spin (S = 1/2), rhombic signals, which are sensitive to changes in the heme-Thiolate H-bonding environment. To establish a well-defined relationship between the magnitude of g-value dispersion in this unique EPR signal and the strength of the heme-Thiolate H-bonding environment, we synthesized and characterized of a series of six-coordinate, aryl-Thiolate-ligated Fe(III) porphyrin complexes bearing a tunable intramolecular H-bond. Spectroscopic investigation of these complexes revealed a direct correlation between H-bond strength and g-value dispersion in the rhombic EPR signal. Using density functional theory (DFT), we elucidated the electronic origins of the narrow, rhombic EPR signal in heme-Thiolates, which arises from an Fe-S pI-dI bonding interaction. Computational analysis of the intramolecularly H-bonded heme-Thiolate models revealed that H-bond donation to the coordinating thiolate reduces thiolate donor strength and weakens this Fe-S interaction, giving rise to larger g-value dispersion. By defining the relationship between heme-Thiolate electronic structure and rhombic EPR signal, it is possible to compare thiolate donor strengths among heme-Thiolate proteins through analysis of low-spin, Fe(III) EPR spectra. Thus, this study establishes EPR spectroscopy as a valuable tool for exploring how second coordination sphere effects influence heme-Thiolate protein function.
Co-Catalyzed Intramolecular S-N Bond Formation in Water for 1,2-Benzisothiazol-3(2H)-ones and 1,2,4-Thiadiazoles Synthesis
Yang, Liting,Song, Lijuan,Tang, Shanyu,Li, Longjia,Li, Heng,Yuan, Bingxin,Yang, Guanyu
, p. 1281 - 1285 (2019/01/14)
An efficient and versatile Co-catalyzed intramolecular S-N bond formation in water to synthesize 1,2-benzisothiazol-3(2H)-one and 1,2,4-thiadiazoles derivatives in good to excellent yields was developed. The transformation showed great tolerance with a broad range of substituents. The mother liquor was able to be recycled 6 times with minor loss in product yield.
Amidation of Carboxylic Acids with Amines by Nb2O5 as a Reusable Lewis Acid Catalyst
Ali,Siddiki,Onodera, Wataru,Kon, Kenichi,Shimizu, Ken-Ichi
, p. 3555 - 3561 (2015/11/10)
Among 28 types of heterogeneous and homogenous catalysts tested, Nb2O5 shows the highest yield for direct amidation of n-dodecanoic acid with a less reactive amine (aniline). The catalytic amidation by Nb2O5 is applicable to a wide range of carboxylic acids and amines with various functional groups, and the catalyst is reusable. A comparison of the results of the catalytic study and an infrared study of the acetic acid adsorbed on the catalyst suggests that activation of the carbonyl group of the carboxylic acid by Lewis acid sites on Nb2O5 is responsible for the high activity of the Nb2O5 catalyst. Kinetic studies show that Lewis acid sites on Nb2O5 are more water-tolerant than conventional Lewis acidic oxides (Al2O3, TiO2). In comparison with the state-of-the-art homogeneous Lewis acid catalyst for amidation (ZrCl4), Nb2O5 undergoes fewer negative effects from basic additives in the solution, which indicates that Nb2O5 is a more base-tolerant Lewis acid catalyst than the homogeneous Lewis acid catalyst.
Design, synthesis and evaluation of benzoisothiazolones as selective inhibitors of PHOSPHO1
Bravo, Yalda,Teriete, Peter,Dhanya, Raveendra-Panickar,Dahl, Russell,Lee, Pooi San,Kiffer-Moreira, Tina,Ganji, Santhi Reddy,Sergienko, Eduard,Smith, Layton H.,Farquharson, Colin,Millan, Jose Luis,Cosford, Nicholas D.P.
, p. 4308 - 4311 (2014/09/17)
We report the discovery and characterization of a series of benzoisothiazolone inhibitors of PHOSPHO1, a newly identified soluble phosphatase implicated in skeletal mineralization and soft tissue ossification abnormalities. High-throughput screening (HTS)
Copper-catalyzed intramolecular N-S bond formation by oxidative dehydrogenative cyclization
Wang, Zhen,Kuninobu, Yoichiro,Kanai, Motomu
, p. 7337 - 7342 (2013/08/15)
Copper-catalyzed synthesis of benzo[d]isothiazol-3(2H)-ones and N-acyl-benzothiazetidine by intramolecular dehydrogenative cyclization is described. In this reaction, a new nitrogen-sulfur (N-S) bond is formed by N-H/S-H coupling. The present reaction has
Reactions of an organoruthenium anticancer complex with 2-mercaptobenzanilide-a model for the active-site cysteine of protein tyrosine phosphatase 1B
Han, Yumiao,Luo, Qun,Hao, Xiang,Li, Xianchan,Wang, Fuyi,Hu, Wenbing,Wu, Kui,Lue, Shuang,Sadler, Peter J.
supporting information; experimental part, p. 11519 - 11529 (2012/01/04)
The organometallic anticancer complex [(η6-p-cymene)Ru(en) Cl]PF6 (1, en = ethylenediamine) readily reacts with thiols and forms stable sulfenate/sulfinate adducts which may be important for its biological activity. Protein tyrosine
Potent, selective, and orally available benzoisothiazolone phosphomannose isomerase inhibitors as probes for congenital disorder of glycosylation Ia
Dahl, Russell,Bravo, Yalda,Sharma, Vandana,Ichikawa, Mie,Dhanya, Raveendra-Panickar,Hedrick, Michael,Brown, Brock,Rascon, Justin,Vicchiarelli, Michael,Mangravita-Novo, Arianna,Yang, Li,Stonich, Derek,Su, Ying,Smith, Layton H.,Sergienko, Eduard,Freeze, Hudson H.,Cosford, Nicholas D. P.
experimental part, p. 3661 - 3668 (2011/06/27)
We report the discovery and validation of a series of benzoisothiazolones as potent inhibitors of phosphomannose isomerase (PMI), an enzyme that converts mannose-6-phosphate (Man-6-P) into fructose-6-phosphate (Fru-6-P) and, more importantly, competes wit
Exploring the structural requirements for inhibition of the ubiquitin E3 ligase breast cancer associated protein 2 (BCA2) as a treatment for breast cancer
Brahemi, Ghali,Kona, Fathima R.,Fiasella, Annalisa,Buac, Daniela,Soukupová, Jitka,Brancale, Andrea,Burger, Angelika M.,Westwell, Andrew D.
supporting information; experimental part, p. 2757 - 2765 (2010/08/20)
The zinc-ejecting aldehyde dehydrogenase (ALDH) inhibitory drug disulfiram (DSF) was found to be a breast cancer-associated protein 2 (BCA2) inhibitor with potent antitumor activity. We herein describe our work in the synthesis and evaluation of new series of zinc-affinic molecules to explore the structural requirements for selective BCA2-inhibitory antitumor activity. An N(C - S)S - S motif was found to be required, based on selective activity in BCA2-expressing breast cancer cell lines and against recombinant BCA2 protein. Notably, the DSF analogs (3a and 3c) and dithio(peroxo)thioate compounds (5d and 5f) were found to have potent activity (submicromolar IC50) in BCA2 positive MCF-7 and T47D cells but were inactive (IC50 > 10 μM) in BCA2 negative MDA-MB-231 breast cancer cells and the normal breast epithelial cell line MCF10A. Testing in the isogenic BCA2 +ve MDA-MB-231/ER cell line restored antitumor activity for compounds that were inactive in the BCA2 -ve MDA-MB-231 cell line. In contrast, structurally related dithiocarbamates and benzisothiazolones (lacking the disulfide bond) were all inactive. Compounds 5d and 5f were additionally found to lack ALDH-inhibitory activity, suggestive of selective E3 ligase-inhibitory activity and worthy of further development.
