購(gòu)物車(chē) 
-
PknG抑制劑
- names：
AX20017
- CAS號(hào)：
329221-38-7
MDL Number： MFCD00785286 - MF(分子式)： C13H16N2O2S MW(分子量)： 264.34
- EINECS: Reaxys Number:
- Pubchem ID:673481 Brand:BIOFOUNT
PknG抑制劑(AX20017,329221-38-7)是蛋白激酶G（PknG）的小分子抑制劑，IC50：0.39μM（PknG)。
| 貨品編碼 | 規(guī)格 | 純度 | 價(jià)格 (￥) | 現(xiàn)價(jià)(￥) | 特價(jià)(￥) | 庫(kù)存描述 | 數(shù)量 | 總計(jì) (￥) |
|---|---|---|---|---|---|---|---|---|
| YZM000167-5mg | 5mg | 99.95% | ￥ 682.50 | ￥ 682.50 | 2-3天 | ￥ 0.00 |
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| 中文別名 | PknG抑制劑(329221-38-7);AX 20017;AX-20017;AX20017; |
| 英文別名 | AX20017(329221-38-7);AX 20017;AX-20017;AX20017;AX 20017;PknG Inhibitor;2-(cyclopropanecarboxamido)-4,5,6,7-tetrahydrobenzo[b]thiophene-3-carboxamide;AX-20017; AX 20017; Mycobacterial Protein Kinase G Inhibitor; 2-(Cyclopropanecarbonylamino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide; PknG Inhibitor ; |
| CAS號(hào) | 329221-38-7 |
| Inchi | InChI=1S/C13H16N2O2S/c14-11(16)10-8-3-1-2-4-9(8)18-13(10)15-12(17)7-5-6-7/h7H,1-6H2,(H2,14,16)(H,15,17) |
| InchiKey | VATFNEMGBRWLHI-UHFFFAOYSA-N |
| 分子式 Formula | C13H16N2O2S |
| 分子量 Molecular Weight | 264.34 |
| 溶解度Solubility | 生物體外In Vitro:DMSO溶解度≥ 32 mg/mL(121.06 mM)*"≥" means soluble可溶, but saturation unknown溶解度未知. |
| 性狀 | 淺褐色固體粉末,Power |
| 儲(chǔ)藏條件 Storage conditions | -20°C 3 years年 4°C 2 years年 / In solvent溶液中:-80°C 6 months月 -20°C 1 month月 |
PknG抑制劑(AX20017,329221-38-7)實(shí)驗(yàn)注意事項(xiàng)：
1.實(shí)驗(yàn)前需戴好防護(hù)眼鏡，穿戴防護(hù)服和口罩，佩戴手套，避免與皮膚接觸。
2.實(shí)驗(yàn)過(guò)程中如遇到有毒或者刺激性物質(zhì)及有害物質(zhì)產(chǎn)生，必要時(shí)實(shí)驗(yàn)操作需要手套箱內(nèi)完成以免對(duì)實(shí)驗(yàn)人員造成傷害
3.實(shí)驗(yàn)后產(chǎn)生的廢棄物需分類(lèi)存儲(chǔ)，并交于專(zhuān)業(yè)生物廢氣物處理公司處理，以免造成環(huán)境污染Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.
Tags：AX20017試劑,AX20017雜質(zhì),AX20017合成,AX20017中間體,AX20017密度,AX20017溶解度,AX20017旋光度,AX20017閃點(diǎn),AX20017熔點(diǎn),AX20017購(gòu)買(mǎi),
| 產(chǎn)品說(shuō)明 | PknG抑制劑(AX20017,329221-38-7)是蛋白激酶G (PknG) 的小分子的抑制劑，IC50值是 0.39 μM |
| Introduction | PknG抑制劑(AX20017,329221-38-7) is a smallolecule protein kinase G (PknG) inhibitor with anIC50of 0.39 μM. |
| Application1 | |
| Application2 | |
| Application3 |
PknG抑制劑(AX20017,329221-38-7)藥理學(xué)：
PknG抑制劑(AX20017,329221-38-7)是一種細(xì)胞可滲透的四氫苯并噻吩化合物，可作為針對(duì)分枝桿菌蛋白激酶G（PknG； IC 50 = 390 nM）的高度特異性和ATP結(jié)合位點(diǎn)靶向抑制劑，而對(duì)其他8種分枝桿菌和25種其他人類(lèi)細(xì)胞則無(wú)活性降低或無(wú)活性激酶，包括與PknG關(guān)系最密切的哺乳動(dòng)物激酶PKCα。已顯示AX20017可以完全滅活PknG介導(dǎo)的溶酶體轉(zhuǎn)移阻滯和巨噬細(xì)胞中牛分枝桿菌 BCG的降解（濃度為10μM或更高），否則不會(huì)影響B(tài)CG在其感染宿主外的生長(zhǎng)。
PknG抑制劑(AX20017,329221-38-7)是一種細(xì)胞可滲透的四氫苯并噻吩化合物，可作為針對(duì)分枝桿菌蛋白激酶G（PknG； IC 50 = 390 nM）的高度特異性和ATP結(jié)合位點(diǎn)靶向抑制劑，而對(duì)其他8種分枝桿菌和25種其他人類(lèi)細(xì)胞則無(wú)活性降低或無(wú)活性激酶，包括與PknG關(guān)系最密切的哺乳動(dòng)物激酶PKCα。已顯示AX20017可以完全滅活PknG介導(dǎo)的溶酶體轉(zhuǎn)移阻滯和巨噬細(xì)胞中牛分枝桿菌 BCG的降解（濃度為10μM或更高），否則不會(huì)影響B(tài)CG在其感染宿主外的生長(zhǎng)。
| 警示圖 | |
| 危險(xiǎn)性 | warning |
| 危險(xiǎn)性警示 | Not available |
| 安全聲明 | H303吞入可能有害+H313皮膚接觸可能有害+H2413吸入可能對(duì)身體有害 |
| 安全防護(hù) | P264處理后徹底清洗+P280戴防護(hù)手套/穿防護(hù)服/戴防護(hù)眼罩/戴防護(hù)面具+P305如果進(jìn)入眼睛+P351用水小心沖洗幾分鐘+P338取出隱形眼鏡（如果有）并且易于操作,繼續(xù)沖洗+P337如果眼睛刺激持續(xù)+P2393獲得醫(yī)療建議/護(hù)理 |
| 備注 | 實(shí)驗(yàn)過(guò)程中防止吸入、食入，做好安全防護(hù) |
| Walburger A, et al. Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science. 2004 Jun 18;304(5678):1800-4. |
| Santhi N, et al. Insights from the molecular docking of withanolide derivatives to the target protein PknG from Mycobacterium tuberculosis. Bioinformation. 2011;7(1):1-4. |
| Scherr N, et al. Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):12151-6. |
PknG抑制劑(AX20017,329221-38-7)參考文獻(xiàn)：
1、Insights from the molecular docking of withanolide derivatives to the target protein PknG from Mycobacterium tuberculosis
Natchimuthu Santhi 1, Sekar Aishwarya
Abstract A crucial virulence factor for intracellular Mycobacterium tuberculosis survival is Protein kinase G (PknG), a eukaryotic-like serinethreonine protein kinase expressed by pathogenic mycobacteria that blocks the intracellular degradation of mycobacteria in lysosomes. Inhibition of PknG results in mycobacterial transfer to lysosomes. Withania somnifera, a reputed herb in ayurvedic medicine, comprises a large number of steroidal lactones known as withanolides which show various pharmacological activities. We describe the docking of 26 withanferin and 14 withanolides from Withania somnifera into the three dimensional structure of PknG of M. tuberculosis using GLIDE. The inhibitor binding positions and affinity were evaluated using scoring functions- Glidescore. The withanolide E, F and D and Withaferin - diacetate 2 phenoxy ethyl carbonate were identified as potential inhibitors of PknG. The available drug molecules and the ligand AX20017 showed hydrogen bond interaction with the aminoacid residues Glu233 and Val235. In addition to Val235 the other amino acids, Gly237, Gln238 and Ser239 are important for withanolide inhibitor recognition via hydrogen bonding mechanisms.
2、Predictive Binding Affinity of Plant-Derived Natural Products Towards the Protein Kinase G Enzyme of Mycobacterium tuberculosis ( Mt PknG)
Rana M Qasaymeh 1, Dino Rotondo 1, Carel B Oosthuizen 2, Namrita Lall 2 3 4, Veronique Seidel
Abstract Tuberculosis (TB), caused by Mycobacterium tuberculosis, is a growing public health concern worldwide, especially with the emerging challenge of drug resistance to the current drugs. Efforts to discover and develop novel, more effective, and safer anti-TB drugs are urgently needed. Products from natural sources, such as medicinal plants, have played an important role in traditional medicine and continue to provide some inspiring templates for the design of new drugs. Protein kinase G, produced by M. tuberculosis (MtPKnG), is a serine/threonine kinase, that has been reported to prevent phagosome-lysosome fusion and help prolong M. tuberculosis survival within the host's macrophages. Here, we used an in silico, target-based approach (docking) to predict the interactions between MtPknG and 84 chemical constituents from two medicinal plants (Pelargonium reniforme and Pelargonium sidoides) that have a well-documented historical use as natural remedies for TB. Docking scores for ligands towards the target protein were calculated using AutoDock Vina as the predicted binding free energies. Ten flavonoids present in the aerial parts of P. reniforme and/or P. sidoides showed docking scores ranging from -11.1 to -13.2 kcal/mol. Upon calculation of all ligand efficiency indices, we observed that the (-?G/MW) ligand efficiency index for flavonoids (4), (5) and (7) was similar to the one obtained for the AX20017 control. When taking all compounds into account, we observed that the best (-?G/MW) efficiency index was obtained for coumaric acid, coumaraldehyde, p-hydroxyphenyl acetic acid and p-hydroxybenzyl alcohol. We found that methyl gallate and myricetin had ligand efficiency indices superior and equal to the AX20017 control efficiency, respectively. It remains to be seen if any of the compounds screened in this study exert an effect in M. tuberculosis-infected macrophages.
3、Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis
Nicole Scherr 1, Srinivas Honnappa, Gabriele Kunz, Philipp Mueller, Rajesh Jayachandran, Fritz Winkler, Jean Pieters, Michel O Steinmetz
Abstract The pathogenicity of mycobacteria such as Mycobacterium tuberculosis is closely associated with their capacity to survive within host macrophages. A crucial virulence factor for intracellular mycobacterial survival is protein kinase G (PknG), a eukaryotic-like serine/threonine protein kinase expressed by pathogenic mycobacteria that blocks the intracellular degradation of mycobacteria in lysosomes. Inhibition of PknG with the highly selective low-molecular-weight inhibitor AX20017 results in mycobacterial transfer to lysosomes and killing of the mycobacteria. Here, we report the 2.4 A x-ray crystal structure of PknG in complex with AX20017. The unique multidomain topology of PknG reveals a central kinase domain that is flanked by N- and C-terminal rubredoxin and tetratrico-peptide repeat domains, respectively. Directed mutagenesis suggests that the rubredoxin domain functions as a regulator of PknG kinase activity. The structure of PknG-AX20017 further reveals that the inhibitor is buried deep within the adenosine-binding site, targeting an active conformation of the kinase domain. Remarkably, although the topology of the kinase domain is reminiscent of eukaryotic kinases, the AX20017-binding pocket is shaped by a unique set of amino acid side chains that are not found in any human kinase. Directed mutagenesis of the unique set of residues resulted in a drastic loss of the compound's inhibitory potency. Our results explain the specific mode of action of AX20017 and demonstrate that virulence factors highly homologous to host molecules can be successfully targeted to block the proliferation of M. tuberculosis.
4、A novel drug discovery concept for tuberculosis: inhibition of bacterial and host cell signalling
Rita Székely 1, Frigyes Wáczek, István Szabadkai, Gábor Németh, Bálint Hegymegi-Barakonyi, Dániel Eros, Bálint Szokol, János Pató, Doris Hafenbradl, Jacqueline Satchell, Brigitte Saint-Joanis, Stewart T Cole, László Orfi, Bert M Klebl, György Kéri
Abstract The Mycobacterium tuberculosis genome encodes for eleven eukaryotic-like Ser/Thr protein kinases. At least three of these (PknA, PknB and PknG) are essential for bacterial growth and survival. PknG is secreted by pathogenic mycobacteria, in macrophages to intervene with host cell signalling pathways and to block the fusion of the lysosomes with the phagosome by a still unknown mechanism. Based on our previously published results, we have initiated a drug discovery program, aiming to improve the potency against PknG and the physiochemical properties of the initially identified hit compound, AX20017, from the class of the tetrahydrobenzothiophenes. We have established a radioactive biochemical PknG kinase assay to test the novel analogues around AX20017. We have developed lead molecules with IC50 values in nanomolar range, and demonstrated their antituberculotic effects on human macrophages. Selected leads might ultimately serve the purpose of inducing phagosomal-lysosomal fusion and therefore destroy the residence of the intracellular mycobacteria. It is unclear at this time if these "homeless" mycobacteria are getting killed by the host, but they will be at least vulnerable to the activity of antimycobacterial agents. Released mycobacteria rely on the essential function of PknB for survival, which is our second molecular kinase target. PknB is a transmembrane protein, responsible for the cell growth and morphology. We have screened our library and synthesized novel compounds for the inhibition of PknB. A pharmacophore model was built and 70,000 molecules from our synthesizable virtual library have been screened to identify novel inhibitor scaffolds for the generation of templated compound libraries. Currently, we are using a radioactive kinase assay employing GarA as the putative, physiological substrate of PknB kinase. We have identified hits and generated optimised hit compounds with IC50 values for the inhibition of PknB in the nanomolar range. Yet those promising hits are not potent enough to yield meaningful "minimum inhibitory concentrations" in mycobacterial growth assays. In the course of our future work, we will increase the potency of the next generation of PknB inhibitors in order to improve their antibacterial activity.
1、Insights from the molecular docking of withanolide derivatives to the target protein PknG from Mycobacterium tuberculosis
Natchimuthu Santhi 1, Sekar Aishwarya
Abstract A crucial virulence factor for intracellular Mycobacterium tuberculosis survival is Protein kinase G (PknG), a eukaryotic-like serinethreonine protein kinase expressed by pathogenic mycobacteria that blocks the intracellular degradation of mycobacteria in lysosomes. Inhibition of PknG results in mycobacterial transfer to lysosomes. Withania somnifera, a reputed herb in ayurvedic medicine, comprises a large number of steroidal lactones known as withanolides which show various pharmacological activities. We describe the docking of 26 withanferin and 14 withanolides from Withania somnifera into the three dimensional structure of PknG of M. tuberculosis using GLIDE. The inhibitor binding positions and affinity were evaluated using scoring functions- Glidescore. The withanolide E, F and D and Withaferin - diacetate 2 phenoxy ethyl carbonate were identified as potential inhibitors of PknG. The available drug molecules and the ligand AX20017 showed hydrogen bond interaction with the aminoacid residues Glu233 and Val235. In addition to Val235 the other amino acids, Gly237, Gln238 and Ser239 are important for withanolide inhibitor recognition via hydrogen bonding mechanisms.
2、Predictive Binding Affinity of Plant-Derived Natural Products Towards the Protein Kinase G Enzyme of Mycobacterium tuberculosis ( Mt PknG)
Rana M Qasaymeh 1, Dino Rotondo 1, Carel B Oosthuizen 2, Namrita Lall 2 3 4, Veronique Seidel
Abstract Tuberculosis (TB), caused by Mycobacterium tuberculosis, is a growing public health concern worldwide, especially with the emerging challenge of drug resistance to the current drugs. Efforts to discover and develop novel, more effective, and safer anti-TB drugs are urgently needed. Products from natural sources, such as medicinal plants, have played an important role in traditional medicine and continue to provide some inspiring templates for the design of new drugs. Protein kinase G, produced by M. tuberculosis (MtPKnG), is a serine/threonine kinase, that has been reported to prevent phagosome-lysosome fusion and help prolong M. tuberculosis survival within the host's macrophages. Here, we used an in silico, target-based approach (docking) to predict the interactions between MtPknG and 84 chemical constituents from two medicinal plants (Pelargonium reniforme and Pelargonium sidoides) that have a well-documented historical use as natural remedies for TB. Docking scores for ligands towards the target protein were calculated using AutoDock Vina as the predicted binding free energies. Ten flavonoids present in the aerial parts of P. reniforme and/or P. sidoides showed docking scores ranging from -11.1 to -13.2 kcal/mol. Upon calculation of all ligand efficiency indices, we observed that the (-?G/MW) ligand efficiency index for flavonoids (4), (5) and (7) was similar to the one obtained for the AX20017 control. When taking all compounds into account, we observed that the best (-?G/MW) efficiency index was obtained for coumaric acid, coumaraldehyde, p-hydroxyphenyl acetic acid and p-hydroxybenzyl alcohol. We found that methyl gallate and myricetin had ligand efficiency indices superior and equal to the AX20017 control efficiency, respectively. It remains to be seen if any of the compounds screened in this study exert an effect in M. tuberculosis-infected macrophages.
3、Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis
Nicole Scherr 1, Srinivas Honnappa, Gabriele Kunz, Philipp Mueller, Rajesh Jayachandran, Fritz Winkler, Jean Pieters, Michel O Steinmetz
Abstract The pathogenicity of mycobacteria such as Mycobacterium tuberculosis is closely associated with their capacity to survive within host macrophages. A crucial virulence factor for intracellular mycobacterial survival is protein kinase G (PknG), a eukaryotic-like serine/threonine protein kinase expressed by pathogenic mycobacteria that blocks the intracellular degradation of mycobacteria in lysosomes. Inhibition of PknG with the highly selective low-molecular-weight inhibitor AX20017 results in mycobacterial transfer to lysosomes and killing of the mycobacteria. Here, we report the 2.4 A x-ray crystal structure of PknG in complex with AX20017. The unique multidomain topology of PknG reveals a central kinase domain that is flanked by N- and C-terminal rubredoxin and tetratrico-peptide repeat domains, respectively. Directed mutagenesis suggests that the rubredoxin domain functions as a regulator of PknG kinase activity. The structure of PknG-AX20017 further reveals that the inhibitor is buried deep within the adenosine-binding site, targeting an active conformation of the kinase domain. Remarkably, although the topology of the kinase domain is reminiscent of eukaryotic kinases, the AX20017-binding pocket is shaped by a unique set of amino acid side chains that are not found in any human kinase. Directed mutagenesis of the unique set of residues resulted in a drastic loss of the compound's inhibitory potency. Our results explain the specific mode of action of AX20017 and demonstrate that virulence factors highly homologous to host molecules can be successfully targeted to block the proliferation of M. tuberculosis.
4、A novel drug discovery concept for tuberculosis: inhibition of bacterial and host cell signalling
Rita Székely 1, Frigyes Wáczek, István Szabadkai, Gábor Németh, Bálint Hegymegi-Barakonyi, Dániel Eros, Bálint Szokol, János Pató, Doris Hafenbradl, Jacqueline Satchell, Brigitte Saint-Joanis, Stewart T Cole, László Orfi, Bert M Klebl, György Kéri
Abstract The Mycobacterium tuberculosis genome encodes for eleven eukaryotic-like Ser/Thr protein kinases. At least three of these (PknA, PknB and PknG) are essential for bacterial growth and survival. PknG is secreted by pathogenic mycobacteria, in macrophages to intervene with host cell signalling pathways and to block the fusion of the lysosomes with the phagosome by a still unknown mechanism. Based on our previously published results, we have initiated a drug discovery program, aiming to improve the potency against PknG and the physiochemical properties of the initially identified hit compound, AX20017, from the class of the tetrahydrobenzothiophenes. We have established a radioactive biochemical PknG kinase assay to test the novel analogues around AX20017. We have developed lead molecules with IC50 values in nanomolar range, and demonstrated their antituberculotic effects on human macrophages. Selected leads might ultimately serve the purpose of inducing phagosomal-lysosomal fusion and therefore destroy the residence of the intracellular mycobacteria. It is unclear at this time if these "homeless" mycobacteria are getting killed by the host, but they will be at least vulnerable to the activity of antimycobacterial agents. Released mycobacteria rely on the essential function of PknB for survival, which is our second molecular kinase target. PknB is a transmembrane protein, responsible for the cell growth and morphology. We have screened our library and synthesized novel compounds for the inhibition of PknB. A pharmacophore model was built and 70,000 molecules from our synthesizable virtual library have been screened to identify novel inhibitor scaffolds for the generation of templated compound libraries. Currently, we are using a radioactive kinase assay employing GarA as the putative, physiological substrate of PknB kinase. We have identified hits and generated optimised hit compounds with IC50 values for the inhibition of PknB in the nanomolar range. Yet those promising hits are not potent enough to yield meaningful "minimum inhibitory concentrations" in mycobacterial growth assays. In the course of our future work, we will increase the potency of the next generation of PknB inhibitors in order to improve their antibacterial activity.
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