Pteryxia terebinthina, Ammi ursina, Musineon diviricatum and Seseli libanotis
>17.1mg/mL in DMSO
486.8±45.0 °C at 760 mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:13161-75-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Selective analogs of the natural glycoside phloridzin are marketed drugs that reduce hyperglycemia in diabetes by inhibiting the active sodium glucose cotransporter SGLT2 in the kidneys. In addition, intestinal SGLT1 is now recognized as a target for glycemic control. To expand available type 2 diabetes remedies, we aimed to find novel SGLT1 inhibitors beyond the chemical space of glycosides. We screened a bioactive compound library for SGLT1 inhibitors and tested primary hits and additional structurally similar molecules on SGLT1 and SGLT2 (SGLT1/2). Novel SGLT1/2 inhibitors were discovered in separate chemical clusters of natural and synthetic compounds. These have IC50-values in the 10-100 μmol/L range. The most potent identified novel inhibitors from different chemical clusters are (SGLT1-IC50 Mean ± SD, SGLT2-IC50 Mean ± SD): (+)-pteryxin (12 ± 2 μmol/L, 9 ± 4 μmol/L), (+)-ε-viniferin (58 ± 18 μmol/L, 110 μmol/L), quinidine (62 μmol/L, 56 μmol/L), cloperastine (9 ± 3 μmol/L, 9 ± 7 μmol/L), bepridil (10 ± 5 μmol/L, 14 ± 12 μmol/L), trihexyphenidyl (12 ± 1 μmol/L, 20 ± 13 μmol/L) and bupivacaine (23 ± 14 μmol/L, 43 ± 29 μmol/L). The discovered natural inhibitors may be further investigated as new potential (prophylactic) agents for controlling dietary glucose uptake. The new diverse structure activity data can provide a starting point for the optimization of novel SGLT1/2 inhibitors and support the development of virtual SGLT1/2 inhibitor screening models.
SGLT1; SGLT2; diabetes; glucose; inhibitors; screening.
Novel natural and synthetic inhibitors of solute carriers SGLT1 and SGLT2
Paul Oranje 1, Robin Gouka 1, Lindsey Burggraaff 2, Mario Vermeer 1, Clement Chalet 1, Guus Duchateau 1, Pieter van der Pijl 1, Marian Geldof 1, Niels de Roo 1, Fenja Clauwaert 3, Toon Vanpaeschen 3, Johan Nicola? 3, Tom de Bruyn 3, Pieter Annaert 3, Adriaan P IJzerman 2, Gerard J P van Westen 2
2019 Jul 30
Pteryxin is a dihydropyranocoumarin derivative found in Apiaceae family. In this study, pteryxin, which was previously isolated from the fruits of Mutellina purpurea, was investigated for its inhibitory potential against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), which are the key enzymes in the pathology of Alzheimer’s disease (AD). The compound was tested in vitro using ELISA microplate reader at 100 μg/ml and found to cause 9.30 ± 1.86% and 91.62 ± 1.53% inhibition against AChE and BChE, respectively. According to our results, pteryxin (IC50 = 12.96 ± 0.70 μg/ml) was found to be a more active inhibitor of BChE than galanthamine (IC50 = 22.16 ± 0.91 μg/ml; 81.93± 2.52% of inhibition at 100 μg/ml). Further study on pteryxin using molecular docking experiments revealed different possible binding modes with both polar and hydrophobic interactions inside the binding pocket of BChE. Top docking solution points out to the formation of two hydrogen bonds with the catalytic residues S198 and H438 of BChE as well as a strong π – π stacking with W231. Therefore, pteryxin as a natural coumarin seems to be a strong BChE inhibitor, which could be considered as a lead compound to develop novel BChE inhibitors for AD treatment.
Alzheimer's disease; Cholinesterase inhibition; Molecular docking; Pteryxin; Pyranocoumarin.
Pteryxin - A promising butyrylcholinesterase-inhibiting coumarin derivative from Mutellina purpurea
Ilkay Erdogan Orhan 1, Fatma Sezer Senol 2, Suhaib Shekfeh 3, Krystyna Skalicka-Wozniak 4, Erden Banoglu 5
3T3-L1 adipocytes; HepG2 hepatocytes; Lipid metabolism; Obesity; Peucedanum japonicum Thunb; Pteryxin.
Pteryxin: a coumarin in Peucedanum japonicum Thunb leaves exerts antiobesity activity through modulation of adipogenic gene network
Ruwani N Nugara 1, Masashi Inafuku 2, Kensaku Takara 3, Hironori Iwasaki 2, Hirosuke Oku 4