Helicid CAS NO.80154-34-3

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General tips：For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging：1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
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Chemical Properties of Helicid

Source of Helicid

The roots of Helicia erratica Hook. f.

Biological Activity of Helicid

Protocol of Helicid

Preparing Stock Solutions of Helicid

References on Helicid

Bioavailability and pharmacokinetics profile of helicid in beagle dogs using gradient elution high performance liquid chromatography electrospray ionization mass spectrometry.[Pubmed:25743699]

J Chromatogr B Analyt Technol Biomed Life Sci. 2015 Apr 15;988:8-12.

A simple, sensitive and reliable gradient elution high performance liquid chromatography electrospray ionization mass spectrometry (HPLC-ESI-MS) method was developed for quantifying Helicid in dog plasma. The limit of detection (LOD) and the lower limit of quantitation (LLOQ) were 0.3 and 1 ng/mL, respectively. This method was validated for selectivity, linearity, accuracy and precision, extraction recoveries, matrix effects, carry-over, cross-talk, dilution integrity, stability and incurred sample reanalysis (ISR). Bioavailability and pharmacokinetic parameters of Helicid in beagle dogs were researched from a two period crossover design study. After intravenous administration (i.v.), Helicid had a mean (+/- SD) AUC0-infinity of 12062.06 +/- 2482.69 ng/mL h and terminal half-life (t1/2 z) of 2.91 +/- 1.37 h, while Cmax was 35613.23 +/- 8157.18 ng/mL. Following intragastric gavage administration (i.g.), AUC0-infinity was 7589.16 +/- 1797.20 ng/mL h along with a longer t1/2 z of 4.10 +/- 4.35 h. Cmax was researched at 0.58 +/- 0.20 h. The absolute bioavailability (F) of Helicid was 15.74 +/- 1.87%.

Synthesis and biological evaluation of helicid analogues as novel acetylcholinesterase inhibitors.[Pubmed:17574306]

Eur J Med Chem. 2008 Jan;43(1):166-73.

A series of Helicid analogues were prepared and evaluated in vitro for the cholinesterase (AChE and BuChE) inhibitory activities via UV spectroscopy. The results indicated that compounds 5, 6d and 8 exhibited potent AChE inhibitory activities with IC(50) values of 0.45+/-0.02microM, 0.49+/-0.02microM, and 0.20+/-0.01microM, respectively. High selectivity for AChE over BuChE was also observed. Kinetic study showed that the mechanism of AChE inhibition of compounds 5, 6d and 8 was all mixed-type.

Synthesis and biological evaluation of helicid analogues as mushroom tyrosinase inhibitors.[Pubmed:18996693]

Bioorg Med Chem Lett. 2008 Dec 15;18(24):6490-3.

A series of Helicid analogues were synthesized and evaluated as tyrosinase inhibitors. The results demonstrated that some compounds had more potent inhibitory activities than arbutin (IC(50) 7.3 mM). In particular, compound 1c bearing 4,6-O-benzylidene substituent on the sugar moiety was found to be the most potent inhibitor with IC(50) value of 0.052 mM. The inhibition kinetics analyzed by Lineweaver-Burk plots revealed that Helicid analogues were competitive inhibitors. The Circular dichroism spectra indicated that those compounds induced conformational changes of mushroom tyrosinase upon binding.

Binding of helicid to human serum albumin: a hybrid spectroscopic approach and conformational study.[Pubmed:24463239]

Spectrochim Acta A Mol Biomol Spectrosc. 2014 Apr 24;124:46-51.

The interaction between human serum albumin and Helicid was studied by steady-state fluorescence, ultraviolet-visible, circular dichroism, Fourier transform infrared techniques and molecular modeling. The binding site numbers, association constants, and corresponding thermodynamic parameters were used to investigate the quenching mechanism. The alternations of protein secondary structure in the presence of Helicid were demonstrated using synchronous fluorescence, Fourier transform infrared, circular dichroism and three-dimensional fluorescence spectra. The molecular modeling results revealed that Helicid could bind to hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. The binding site of Helicid in HSA was ascertained. Moreover, an apparent distance of 3.33 nm between the Trp214 and Helicid was obtained via fluorescence resonance energy transfer method.

Description

Helicid (Helicide) is a major constituent of Helicia nilgirica Bedd. Helicid has been used to treat psychoneurosis for its sedative-hypnotic and analgesic properties.

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