5332-70-7Relevant academic research and scientific papers
Use of azidonaphthalimide carboxylic acids as fluorescent templates with a built-in photoreactive group and a flexible linker simplifies protein labeling studies: Applications in selective tagging of HCAII and penicillin binding proteins
Singha, Monisha,Roy, Sayantani,Pandey, Satya Deo,Bag, Subhendu Sekhar,Bhattacharya, Prabuddha,Das, Mainak,Ghosh, Anindya S.,Ray, Debashis,Basak, Amit
, p. 13015 - 13018 (2017)
This work describes the synthesis of azidonaphthalimide carboxylic acids which act as fluorescent templates with a built-in photoreactive group and a linker thus simplifying the design of protein labeling agents. These were separately connected to selecti
Inhibition of Carbonic Anhydrase Using SLC-149: Support for a Noncatalytic Function of CAIX in Breast Cancer
Mboge, Mam Y.,Combs, Jacob,Singh, Srishti,Andring, Jacob,Wolff, Alyssa,Tu, Chingkuang,Zhang, Zaihui,McKenna, Robert,Frost, Susan C.
supporting information, p. 1713 - 1724 (2021/02/16)
Carbonic anhydrase IX (CAIX) is considered a target for therapeutic intervention in solid tumors. In this study, the efficacy of the inhibitor, 4-(3-(2,4-difluorophenyl)-oxoimidazolidin-1-yl)benzenesulfonamide (SLC-149), is evaluated on CAIX and a CAIX-mimic. We show that SLC-149 is a better inhibitor than acetazolamide against CAIX. Binding of SLC-149 thermally stabilizes CAIX-mimic at lower concentrations compared to that of CAII. Structural examinations of SLC-149 bound to CAIX-mimic and CAII explain binding preferences. In cell culture, SLC-149 is a more effective inhibitor of CAIX activity in a triple-negative breast cancer cell line than previously studied sulfonamide inhibitors. SLC-149 is also a better inhibitor of activity in cells expressing CAIX versus CAXII. However, SLC-149 has little effect on cytotoxicity, and high concentrations are required to inhibit cell growth, migration, and invasion. These data support the hypothesis that CAIX activity, shown to be important in regulating extracellular pH, does not underlie its ability to control cell growth.
Identification of N-phenyl-2-(phenylsulfonyl)acetamides/propanamides as new SLC-0111 analogues: Synthesis and evaluation of the carbonic anhydrase inhibitory activities
Elbadawi, Mostafa M.,Eldehna, Wagdy M.,Nocentini, Alessio,Abo-Ashour, Mahmoud F.,Elkaeed, Eslam B.,Abdelgawad, Mohamed A.,Alharbi, Khalid S.,Abdel-Aziz, Hatem A.,Supuran, Claudiu T.,Gratteri, Paola,Al-Sanea, Mohammad M.
, (2021/03/30)
As a front-runner selective CA IX inhibitor currently in Phase Ib/II clinical trials, SLC-0111 has been herein exploited as a lead molecule for development of new different sets of N-phenyl-2-(phenylsulfonyl)acetamides/propanamides incorporating different functionalities; primary sulfonamide (5a-f), free carboxylic (8a, 8d), ethyl ester (8b, 8e), acetyl (8c, 8f) and nitro (10a, 10b), as potential carbonic anhydrase (CA, EC 4.2.1.1) inhibitors. All the prepared analogues have been examined for their CA inhibitory activities towards four human (h) isoenzymes, hCA I, II, IX and XII. Interestingly, replacement of SLC-0111 ureido linker with the flexible sulfonyl acetamide linker, as well as linker branching and elongation strategies successfully enhanced the inhibitory action toward hCA IX isoform, such as in sulfones 5a-d and 5f which displayed better activity than SLC-0111. Furthermore, sulfonamide-based sulfone (5f) and carboxylic acid-based sulfones (8a and 8d) demonstrated interesting selectivity toward the tumor-related hCA IX isoform over both hCA I and hCA II, which suggests them as promising candidates for further development as potential anticancer candidates. Thereafter, the anti-proliferative action for sulfones 5f, 8a and 8d was examined against breast (MCF-7) and colon (HCT-116) cancer cell lines. Also, sulfone 5f was further assessed for its impact on the cell cycle progression and apoptosis in HCT-116 cells.
Discovery of novel artemisinin-sulfonamide hybrids as potential carbonic anhydrase IX inhibitors with improved antiproliferative activities
An, Ran,Lin, Bin,Zhao, Shuang,Cao, Chun,Wang, Yuanxin,Cheng, Xue,Liu, Yichuang,Guo, Mengbi,Xu, Hang,Wang, Yitong,Hou, Zhuang,Guo, Chun
supporting information, (2020/10/18)
A series of artemisinin-sulfonamide hybrids (1–16) have been designed and synthesized by using molecular hybridization approach and investigated for the inhibitory activity of four human (h) carbonic anhydrases (CAs, EC 4.2.1.1), hCA I, II, IX and XII. Th
ARYL SULFONAMIDE COMPOUNDS AS CARBONIC ANHYDRASE INHIBITORS AND THEIR THERAPEUTIC USE
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Page/Page column 42, (2017/01/23)
Disclosed herein are compounds having the following structure useful as inhibitors of carbonic anhydrase IX (CAIX) and XII, and particularly useful for reducing or eliminating metastases see Formula (I).
Synthesis and biological properties of novel pyridinioalkanoyl thiolesters (PATE) as anti-HIV-1 agents that target the viral nucleocapsid protein zinc fingers
Turpin, Jim A.,Song, Yongsheng,Inman, John K.,Huang, Mingjun,Wallqvist, Anders,Maynard, Andrew,Covell, David G.,Rice, William G.,Ettore, Appella
, p. 67 - 86 (2007/10/03)
Nucleocapsid p7 protein (NCp7) zinc finger domains of the human immunodeficiency virus type 1 (HIV-1) are being developed as antiviral targets due to their key roles in vital replication and their mutationally nonpermissive nature. On the basis of our exp
