CPS2 - CAS 2756741-90-7

CPS2 is a first-in-class, highly potent, selective and irreversible PROTAC CDK2 degrader (IC50 = 24 nM) for the study of acute myeloid leukemia.

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Molecular Formula
C38H42N12O10S2
Molecular Weight
890.94

CPS2

    • Specification
      • Purity
        ≥95%
        Solubility
        Soluble in DMSO
        Appearance
        White to Beige Powder
        Storage
        Store at 2-8°C
        IUPAC Name
        4-[[5-amino-1-(3-methylthiophene-2-carbonyl)-1,2,4-triazol-3-yl]amino]-N-[2-[[1-[2-[2-[2-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]ethoxy]ethoxy]ethyl]triazol-4-yl]methoxy]ethyl]benzenesulfonamide
        Synonyms
        4-((5-amino-1-(3-methylthiophene-2-carbonyl)-1H-1,2,4-triazol-3-yl)amino)-N-(2-((1-(2-(2-(2-((2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindolin-4-yl)amino)ethoxy)ethoxy)ethyl)-1H-1,2,3-triazol-4-yl)methoxy)ethyl)benzenesulfonamide; CDK2 degrader CPS2; Benzenesulfonamide, 4-[[5-amino-1-[(3-methyl-2-thienyl)carbonyl]-1H-1,2,4-triazol-3-yl]amino]-N-[2-[[1-[2-[2-[2-[[2-(2,6-dioxo-3-piperidinyl)-2,3-dihydro-1,3-dioxo-1H-isoindol-4-yl]amino]ethoxy]ethoxy]ethyl]-1H-1,2,3-triazol-4-yl]methoxy]ethyl]-; 4-[[5-Amino-1-[(3-methyl-2-thienyl)carbonyl]-1H-1,2,4-triazol-3-yl]amino]-N-[2-[[1-[2-[2-[2-[[2-(2,6-dioxo-3-piperidinyl)-2,3-dihydro-1,3-dioxo-1H-isoindol-4-yl]amino]ethoxy]ethoxy]ethyl]-1H-1,2,3-triazol-4-yl]methoxy]ethyl]benzenesulfonamide
    • Properties
      • Density
        1.62±0.1 g/cm3
        InChI Key
        BXCPYBFBMAWDDY-UHFFFAOYSA-N
        InChI
        InChI=1S/C38H42N12O10S2/c1-23-11-20-61-32(23)36(55)50-37(39)44-38(46-50)42-24-5-7-26(8-6-24)62(56,57)41-13-16-60-22-25-21-48(47-45-25)14-17-59-19-18-58-15-12-40-28-4-2-3-27-31(28)35(54)49(34(27)53)29-9-10-30(51)43-33(29)52/h2-8,11,20-21,29,40-41H,9-10,12-19,22H2,1H3,(H,43,51,52)(H3,39,42,44,46)
        Canonical SMILES
        CC1=C(SC=C1)C(=O)N2C(=NC(=N2)NC3=CC=C(C=C3)S(=O)(=O)NCCOCC4=CN(N=N4)CCOCCOCCNC5=CC=CC6=C5C(=O)N(C6=O)C7CCC(=O)NC7=O)N
    • Reference Reading
      • 1. Prevalence of Streptococcus suis genotypes in wild boars of Northwestern Germany
        Martin Beyerbach, Gerd Josef Verkühlen, Peter Valentin-Weigand, Luciana M G Silva, Thomas Rehm, Klaus Pohlmeyer, Christoph G Baums Appl Environ Microbiol . 2007 Feb;73(3):711-7. doi: 10.1128/AEM.01800-06.
        Invasive serotype 2 (cps2+) strains of Streptococcus suis cause meningitis in pigs and humans. Four case reports of S. suis meningitis in hunters suggest transmission of S. suis through the butchering of wild boars. Therefore, the objective of this study was to investigate the prevalence of potentially human-pathogenic S. suis strains in wild boars. S. suis was isolated from 92% of all tested tonsils (n=200) from wild boars. A total of 244 S. suis isolates were genotyped using PCR assays for the detection of serotype-specific genes, the hemolysin gene sly, and the virulence-associated genes mrp and epf. The prevalence of the cps2+ genotype among strains from wild boars was comparable to that of control strains from domestic pig carriers. Ninety-five percent of the cps2+ wild boar strains were positive for mrp, sly, and epf*, the large variant of epf. Interestingly, epf* was significantly more frequently detected in cps2+ strains from wild boars than in those from domestic pigs; epf* is also typically found in European S. suis isolates from humans, including a meningitis isolate from a German hunter. These results suggest that at least 10% of wild boars in Northwestern Germany carry S. suis strains that are potentially virulent in humans. Additional amplified fragment length polymorphism analysis supported this hypothesis, since homogeneous clustering of the epf* mrp+ sly+ cps2+ strains from wild boars with invasive human and porcine strains was observed.
        2. Fighting Antibiotic-Resistant Klebsiella pneumoniae with "Sweet" Immune Targets
        Roberto Adamo, Immaculada Margarit mBio . 2018 May 15;9(3):e00874-18. doi: 10.1128/mBio.00874-18.
        Antibiotics and vaccines have greatly impacted human health in the last century by dramatically reducing the morbidity and mortality associated with infectious diseases. The recent challenge posed by the emergence of multidrug-resistant bacteria could possibly be addressed by novel immune prophylactic and therapeutic approaches. Among the newly threatening pathogens,Klebsiella pneumoniaeis particularly worrisome in the nosocomial setting, and its surface polysaccharides are regarded as promising antigen candidates. The majority ofKlebsiellacarbapenem-resistant strains belong to the sequence type 158 (ST258) lineage, with two main clades expressing capsular polysaccharides CPS1 and CPS2. In a recent article, S. D. Kobayashi and colleagues (mBio 9:e00297-18, 2018, https://doi.org/10.1128/mBio.00297-18) show that CPS2-specific IgGs render ST258 clade 2 bacteria more sensitive to human serum and phagocytic killing. E. Diago-Navarro et al. (mBio 9:e00091-18, 2018, https://doi.org/10.1128/mBio.00091-18) generated two murine monoclonal antibodies recognizing distinct glycotopes of CPS2 that presented functional activity against multiple ST258 strains. These complementary studies represent a step toward the control of this dangerous pathogen.
        3. Clostridium perfringens Virulent Bacteriophage CPS2 and Its Thermostable Endolysin LysCPS2
        Bokyung Son, Sangryeol Ryu, Eunsu Ha Viruses . 2018 May 11;10(5):251. doi: 10.3390/v10050251.
        Clostridium perfringensis one of the most common causes of food-borne illness. The increasing prevalence of multidrug-resistant bacteria requires the development of alternatives to typical antimicrobial treatments. Here, we isolated and characterized aC. perfringens-specific virulent bacteriophage CPS2 from chicken feces. The CPS2 phage contains a 17,961 bp double-stranded DNA genome with 25 putative ORFs, and belongs to thePicovirinae, subfamily ofPodoviridae. Bioinformatic analysis of the CPS2 genome revealed a putative endolysin, LysCPS2, which is homologous to the endolysin ofClostridiumphage phiZP2 and phiCP7R. The enzyme showed strong lytic activity againstC. perfringenswith optimum conditions at pH 7.5⁻10, 25⁻65 °C, and over a broad range of NaCl concentrations. Interestingly, LysCPS2 was found to be highly thermostable, with up to 30% of its lytic activity remaining after 10 min of incubation at 95 °C. The cell wall binding domain in the C-terminal region of LysCPS2 showed a binding spectrum specific toC. perfringensstrains. This is the first report to characterize highly thermostable endolysin isolated from virulentC. perfringensbacteriophage. The enzyme can be used as an alternative biocontrol and detection agent againstC. perfringens.
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