Plant iridoid glycosides and phytogrowth-inhibitory activity of Verbascum virgatum

2004 ◽  
Vol 32 (3) ◽  
pp. 367-370 ◽  
Author(s):  
Fernando Pardo ◽  
Fernando Perich ◽  
René Torres ◽  
Franco Delle Monache
2020 ◽  
Vol 169 ◽  
pp. 112185 ◽  
Author(s):  
Toshio Morikawa ◽  
Yusuke Nakanishi ◽  
Naoki Inoue ◽  
Yoshiaki Manse ◽  
Hideyuki Matsuura ◽  
...  

2020 ◽  
pp. 1-7
Author(s):  
Gui-Min Xue ◽  
Chen-Guang Zhao ◽  
Jin-Feng Xue ◽  
Zhen-Zhu Zhao ◽  
Ying-Ying Si ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5867
Author(s):  
Jun Hee Park ◽  
Wan Kyunn Whang

Previous studies have reported that Hedyotis diffusa Willdenow extract shows various biological activities on cerebropathia, such as neuroprotection and short-term memory enhancement. However, there has been a lack of studies on the inhibitory activity on neurodegenerative diseases such as Alzheimer’s disease (AD) through enzyme assays of H. diffusa. Therefore, H. diffusa extract and fractions were evaluated for their inhibitory effects through assays of enzymes related to AD, including acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), and β-site amyloid precursor protein cleaving enzyme 1 (BACE1), and on the formation of advanced glycation end-product (AGE). In this study, ten bioactive compounds, including nine iridoid glycosides 1–9 and one flavonol glycoside 10, were isolated from the ethyl acetate and n-butanol fractions of H. diffusa using a bioassay-guided approach. Compound 10 was the strongest inhibitor of cholinesterase, BACE1, and the formation of AGEs of all isolated compounds, while compound 5 had the lowest inhibitory activity. Compounds 3, 6, and 9 exhibited better inhibitory activity than other compounds on AChE, and two pairs of diastereomeric iridoid glycoside structures (compounds 4, 8, and 6, 7) showed higher inhibitory activity than others on BChE. In the BACE1 inhibitory assay, compounds 1–3 were good inhibitors, and compound 10 showed higher inhibitory activity than quercetin, the positive control. Moreover, compounds 1 and 3 were stronger inhibitors of the formation of AGE than aminoguanidine (AMG), the positive control. In conclusion, this study is significant since it demonstrated that the potential inhibitory activity of H. diffusa on enzymes related to AD and showed the potential use for further study as a natural medicine for AD treatment on the basis of the bioactive components isolated from H. diffusa.


2017 ◽  
Vol 22 ◽  
pp. 261-265
Author(s):  
Jiao-xian Cao ◽  
Rui An ◽  
Ying Tang ◽  
Han-chuan Yu ◽  
Ying-chun Wu ◽  
...  

Author(s):  
Pınar Ercan ◽  
Sedef Nehir El

Abstract. The goals of this study were to determine and evaluate the bioaccessibility of total anthocyanin and procyanidin in apple (Amasya, Malus communis), red grape (Papazkarası, Vitis vinifera) and cinnamon (Cassia, Cinnamomum) using an in vitro static digestion system based on human gastrointestinal physiologically relevant conditions. Also, in vitro inhibitory effects of these foods on lipid (lipase) and carbohydrate digestive enzymes (α-amylase and α-glucosidase) were performed with before and after digested samples using acarbose and methylumbelliferyl oleate (4MUO) as the positive control. While the highest total anthocyanin content was found in red grape (164 ± 2.51 mg/100 g), the highest procyanidin content was found in cinnamon (6432 ± 177.31 mg/100 g) (p < 0.05). The anthocyanin bioaccessibilities were found as 10.2 ± 1%, 8.23 ± 0.64%, and 8.73 ± 0.70% in apple, red grape, and cinnamon, respectively. The procyanidin bioaccessibilities of apple, red grape, and cinnamon were found as 17.57 ± 0.71%, 14.08 ± 0.74% and 18.75 ± 1.49%, respectively. The analyzed apple, red grape and cinnamon showed the inhibitory activity against α-glucosidase (IC50 544 ± 21.94, 445 ± 15.67, 1592 ± 17.58 μg/mL, respectively), α-amylase (IC50 38.4 ± 7.26, 56.1 ± 3.60, 3.54 ± 0.86 μg/mL, respectively), and lipase (IC50 52.7 ± 2.05, 581 ± 54.14, 49.6 ± 2.72 μg/mL), respectively. According to our results apple, red grape and cinnamon have potential to inhibit of lipase, α-amylase and α-glucosidase digestive enzymes.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
M Ishibashi ◽  
S Hanazawa ◽  
Y Uchino ◽  
X Li ◽  
MA Arai

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
EJ Jeong ◽  
HJ Yang ◽  
KY Lee ◽  
HK Yang ◽  
SH Kim ◽  
...  

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