Territrem B
(Synonyms: 土震素B) 目录号 : GC40023A mycotoxin and AChE inhibitor
Cas No.:70407-20-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Territrem B is a mycotoxin originally isolated from A. terreus that irreversibly inhibits acetylcholinesterase (AChE; IC50 = 19 nM for the electric eel enzyme). It induces tremors in mice with a median tremulous dose of 0.21 mg/kg.
| Cas No. | 70407-20-4 | SDF | |
| 别名 | 土震素B | ||
| Canonical SMILES | O=C1C=CC(C)(C)[C@]([C@@]21C)(O)CC[C@@]([C@]2(O)C3)(C)OC4=C3C(OC(C5=CC(OC)=C(OC)C(OC)=C5)=C4)=O | ||
| 分子式 | C29H34O9 | 分子量 | 526.6 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.899 mL | 9.4949 mL | 18.9897 mL |
| 5 mM | 0.3798 mL | 1.899 mL | 3.7979 mL |
| 10 mM | 0.1899 mL | 0.9495 mL | 1.899 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Production of polyclonal antibodies against Territrem B and detection of Territrem B in the conidia of Aspergillus terreus 23-1 by immunoelectron microscopy
J Agric Food Chem 2004 Jun 2;52(11):3360-5.PMID:15161198DOI:10.1021/jf030787n.
Territrem B, a fungal metabolite isolated from Aspergillums terreus 23-1, is a tremorgenic mycotoxin. Immunoelectron microscopy using anti-territrem B polyclonal antibody was used to detect Territrem B in the fungal body of A. terreus 23-1 at different times of culture without shaking on potato dextrose (PD) agar medium. The anti-territrem B serum was produced by immunization of rabbits with 4beta-hydroxymethyl-4beta-demethylterritrem B-sccinate bound by a linker to keyhole limpet hemocyanin. This antiserum recognized territrems and immunoelectron microscopy using this antiserum, and colloidal gold-conjugated anti-rabbit IgG antibodies showed that Territrem B was localized to the fungal body of A. terreus 23-1. Territrem B was first seen in the cytoplasm of the conidia after 4 days' culture on PD agar medium. Maximal Territrem B production in the conidia was seen on the 14th day of culture; however, Territrem B was not formed in the hyphae at any stage of culture. These results are consistent with the previous finding that the formation of territrems is related to fungal sporulation.
Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and Territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination
J Mol Neurosci 2014 Jul;53(3):506-10.PMID:24573600DOI:10.1007/s12031-014-0261-3.
Acetylcholinesterase (AChE) is a critical enzyme that regulates neurotransmission by degrading the neurotransmitter acetylcholine in synapses of the nervous system. It is an important target for both therapeutic drugs that treat Alzheimer's disease and organophosphate (OP) chemical warfare agents that cripple the nervous system and cause death through paralysis. We are exploring a strategy to design compounds that bind tightly at or near a peripheral or P-site near the mouth of the AChE active site gorge and exclude OPs from the active site while interfering minimally with the passage of acetylcholine. However, to target the AChE P-site, much more information must be gathered about the structure-activity relationships of ligands that bind specifically to the P-site. Here, we review our recent reports on two uncharged, natural product inhibitors of AChE, dihydrotanshinone I and Territrem B, that have relatively high affinities for the enzyme. We describe an inhibitor competition assay and comment on the structures of these inhibitors in complex with recombinant human acetylcholinesterase as determined by X-ray crystallography. Our results reveal that dihydrotanshinone I binding is specific to only the P-site, while Territrem B binding spans the P-site and extends into the acylation or A-site at the base of the gorge.
Territrem B, a tremorgenic mycotoxin that inhibits acetylcholinesterase with a noncovalent yet irreversible binding mechanism
J Biol Chem 1999 Dec 3;274(49):34916-23.PMID:10574966DOI:10.1074/jbc.274.49.34916.
Territrem B (TRB) is a fungal metabolite isolated from Aspergillus terreus shown previously to be a potent and irreversible inhibitor of acetylcholinesterase (AChE). In the present study, a number of binding and inhibition assays were carried out to further characterize the inhibitory effect of TRB. The results indicate that the binding of TRB (a) is much more selective than a well characterized selective inhibitor of AChE, BW284C51, (b) adopts a one-to-one stoichiometry with the enzyme, (c) cannot be undone by an AChE-regenerating oxime agent, which contrasts the ability of 8 M urea to release AChE-bound TRB, (d) is enhanced by high concentration NaCl but prevented, unless preincubated, by Triton X-100, and (e) exhibits quasi-first order kinetics with an overall inhibition constant of 0.01 nM(-1) min(-1). Together these results suggest a very different irreversible binding (a noncovalent type) from that of the covalent type, which involves typical irreversible AChE inhibitors such as diisopropylfluorophosphate and neostigmine. According to the prediction of a molecular modeling study, the distinct AChE inhibitory characteristics of TRB may arise from the inhibitor being noncovalently trapped within a unique active-site gorge structure of the enzyme. It was predicted that an optimal TRB. AChE binding would position a narrowing connection of the TRB structure at a constricted area near the entrance of the gorge, thereby providing a structural basis for the observed irreversible binding.
Acetylcholinesterase inhibition by Territrem B derivatives
J Nat Prod 1995 Jun;58(6):857-62.PMID:7673929DOI:10.1021/np50120a006.
Five derivatives of Territrem B [2], a potent acetylcholinesterase inhibitor isolated from a rice culture of Aspergillus terreus, were prepared from 2 as well as from its major metabolite, 4 beta-hydroxymethyl-4 beta-demethylterritrem B [4]. The inhibitory activities of these derivatives against electric eel acetylcholinesterase (E.C. 3.1.1.7) were tested and it was concluded that the enone and the pyrone groups present in 2 may play an important biological role.
Isolation, chemical structure, acute toxicity, and some physicochemical properties of Territrem B' from Aspergillus terreus
Appl Environ Microbiol 1985 Mar;49(3):721-3.PMID:3994375DOI:10.1128/aem.49.3.721-723.1985.
We have isolated a metabolite of territrem, designated Territrem B', from the chloroform extract of a rice culture of Aspergillus terreus 23-1 by using the same isolation procedure as that for territrems A, B, and C. The present isolation procedure gave about 10 mg of Territrem B' from 4 kg of rice culture per batch. Analysis of the high-resolution mass spectrum showed that the molecular composition of Territrem B' is C29H34O10 (found, 542.2167; required, 542.200). Some results of physicochemical and acute tests are presented in this paper. Single-crystal X-ray diffractometry of Territrem B' indicated that the three-dimensional structure of Territrem B' has not changed significantly from that of Territrem B except for the insertion of one oxygen atom into Territrem B to make an additional pyron ring in the E ring. The tremorgenic activity of Territrem B' is greatly reduced as tested by intraperitoneal injection in mice.