Name: CPS2
Brand: BOC Sciences
Rating: 5 (1 reviews)

Purity

≥95%

Solubility

Soluble in DMSO

Appearance

White to Beige Powder

Storage

Store at 2-8°C

IUPACName

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

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)

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

Mechanism

Target: CPS2 selectively targets cyclin-dependent kinase 2 for proteasomal degradation.

Binding site: Its CDK2-directed ligand engages the kinase ATP-binding catalytic pocket.

Mechanism of action: CPS2 is a selective CDK2-directed PROTAC reported as an irreversible degrader for targeted protein degradation studies. The molecule contains a CDK2-recognition ligand, linker, and CRBN-recruiting ligand, allowing recruitment of CDK2 to cereblon-containing E3 ubiquitin ligase machinery. This proximity promotes CDK2 ubiquitination and subsequent proteasomal degradation, enabling functional studies that remove both catalytic and noncatalytic roles of CDK2. CPS2 is useful for evaluating CDK2 dependency, cell-cycle regulation, differentiation-associated signaling, and the experimental distinction between kinase inhibition and full protein depletion.

Applications

• PROTAC-Mediated Oncoprotein Degradation: CPS2 is utilized in research to selectively degrade oncogenic proteins, offering insights into cancer biology and potential therapeutic targets. By harnessing the body's ubiquitin-proteasome system, CPS2 facilitates the removal of specific proteins, aiding in the study of tumor progression and cellular responses to protein degradation.

• Targeted Kinase Degradation: Researchers employ CPS2 to degrade specific kinases implicated in disease pathways. This application allows for the exploration of kinase function and regulation, enabling the identification of novel intervention points in signaling cascades through the precise elimination of target proteins.

• Protein Homeostasis Regulation via PROTAC: CPS2 serves as a tool for studying cellular protein homeostasis by degrading aberrant or misfolded proteins. This application is crucial for understanding diseases characterized by protein aggregation, offering a platform for investigating mechanisms of protein quality control and cellular health maintenance.

• E3 Ligase Recruitment Studies: CPS2 aids in the investigation of E3 ligase recruitment dynamics, providing valuable data on ligase-substrate interactions. By modulating the degradation of target proteins, researchers can dissect the role of specific E3 ligases in protein turnover and cellular regulation, advancing the field of targeted protein degradation.

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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