|Source:||The herbs of Lycopodium serratum|
|Biological Activity or Inhibitors:||1. Huperzine-B is a efficient inhibitor of human brain AChE.
2. Huperzine-B can enhance ognitive and protect neuro, may be potentially new drug candidates for Alzheimer's disease therapy.
|Solvent:||Chloroform, Dichloromethane, Ethyl Acetate, DMSO, Acetone, etc.|
|Storage:||Providing storage is as stated on the product vial and the vial is kept tightly sealed, the product can be stored for up to 24 months(2-8C).
Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20C. Generally, these will be useable for up to two weeks. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour.
Need more advice on solubility, usage and handling? Please email to: email@example.com
|After receiving:||The packaging of the product may have turned upside down during transportation, resulting in the natural compounds adhering to the neck or cap of the vial. take the vial out of its packaging and gently shake to let the compounds fall to the bottom of the vial. for liquid products, centrifuge at 200-500 RPM to gather the liquid at the bottom of the vial. try to avoid loss or contamination during handling.|
|1 mg||5 mg||10 mg||20 mg||25 mg|
|1 mM||3.9009 mL||19.5046 mL||39.0092 mL||78.0183 mL||97.5229 mL|
|5 mM||0.7802 mL||3.9009 mL||7.8018 mL||15.6037 mL||19.5046 mL|
|10 mM||0.3901 mL||1.9505 mL||3.9009 mL||7.8018 mL||9.7523 mL|
|50 mM||0.078 mL||0.3901 mL||0.7802 mL||1.5604 mL||1.9505 mL|
|100 mM||0.039 mL||0.195 mL||0.3901 mL||0.7802 mL||0.9752 mL|
CNS Neurol Disord Drug Targets. 2014 Apr;13(3):487-90.
|Molecular interaction of human brain acetylcholinesterase with a natural inhibitor huperzine-B: an enzoinformatics approach.[Pubmed: 24059299]|
|The present study emphasizes the molecular interactions between human brain acetylcholinesterase (AChE) and the natural ligand Huperzine B and its comparison to 'AChE-Tolserine interactions'. Docking between Huperzine B and AChE was performed using 'Autodock4.2'. Hydrophobic interactions and hydrogen bonds both play an equally important role in the correct positioning of Huperzine B within the 'catalytic site' of AChE to permit docking. However, docking of Tolserine to AChE is largely dominated by hydrophobic interactions. Such information may aid in the design of versatile AChE-inhibitors, and is expected to aid in safe clinical use of Huperzine B. Scope still remains in the determination of the three-dimensional structure of AChE-Huperzine B complex by X-ray crystallography to validate the described data. Furthermore, this study confirms that Huperzine B is a more efficient inhibitor of human brain AChE compared to tolserine with reference to Ki and ΔG values.|
Acta Pharmacol Sin. 2009 Aug;30(8):1195-203.
|Novel 16-substituted bifunctional derivatives of huperzine B: multifunctional cholinesterase inhibitors.[Pubmed: 19578388]|
|AIM: To design novel bifunctional derivatives of Huperzine B (HupB) based on the concept of dual binding site of acetylcholinesterase (AChE) and evaluate their pharmacological activities for seeking new drug candidates against Alzheimer's disease (AD). METHODS: Novel 16-substituted bifunctional derivatives of Huperzine B were synthesized through chemical reactions. The inhibitory activities of the derivatives toward AChE and butyrylcholinesterase (BuChE) were determined in vitro by modified Ellman's method. Cell viability was quantified by the reduction of MTT. RESULTS: A new preparative method was developed for the generation of 16-substituted derivatives of Huperzine B, and pharmacological trials indicated that the derivatives were multifunctional cholinesterase inhibitors targeting both AChE and BuChE. Among the derivatives tested, 9c, 9e, 9f, and 9i were 480 to 1360 times more potent as AChE inhibitors and 370 to 1560 times more potent as BuChE inhibitors than the parent Huperzine B. Further preliminary pharmacological trials of derivatives 9c and 9i were performed, including examining the mechanism of AChE inhibition, the substrate kinetics of the enzyme inhibition, and protection against hydrogen peroxide (H2O2)-induced cytotoxicity in PC12 cells. CONCLUSION: Preliminary pharmacological evaluation indicated that 16-substituted derivatives of Huperzine B, particularly 9c and 9i, would be potentially valuable new drug candidates for AD therapy, and further exploration is needed to evaluate their pharmacological and clinical efficacies.|
Bioorg Med Chem. 2007 Feb 1;15(3):1394-408.
|Study on dual-site inhibitors of acetylcholinesterase: Highly potent derivatives of bis- and bifunctional huperzine B.[Pubmed: 17126020]|
|Natural (-)-Huperzine B (HupB), isolated from Chinese medicinal herb, displayed moderate inhibitory activity of acetylcholinesterase (AChE). Based on the active dual-site of AChE, a series of novel derivatives of bis- and bifunctional Huperzine B were designed and synthesized. The AChE inhibition potency of most derivatives of Huperzine B was enhanced about 2-3 orders of magnitude as compared with the parental Huperzine B. Among bis-Huperzine B derivatives, 12h exhibited the most potent in the AChE inhibition and has been evaluated for its pharmacological actions in vivo on ChE inhibition, cognitive enhancement, and neuroprotection. The docking study on the bis-Huperzine B derivatives 12 series with TcAChE has demonstrated that the ligands bound to the dual-site of the enzyme in different level.|
Bioorg Med Chem Lett. 2005 Feb 1;15(3):523-6.
|Synthesis and acetylcholinesterase inhibition of derivatives of huperzine B.[Pubmed: 15664805]|
|By targeting dual active sites of AChE, a number of new derivatives of Huperzine B have been synthesized and tested as acetylcholinesterase inhibitors. The most potent compound, bis-Huperzine B 5b is 72-fold more potent in AChE inhibition and 79-fold more selective for AChE versus BChE than Huperzine B.|