scholarly journals Natural α-Glucosidase and Protein Tyrosine Phosphatase 1B Inhibitors: A Source of Scaffold Molecules for Synthesis of New Multitarget Antidiabetic Drugs

Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 4818
Author(s):  
Massimo Genovese ◽  
Ilaria Nesi ◽  
Anna Caselli ◽  
Paolo Paoli
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Antidiabetic Drugs ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Lead Compounds ◽  
Limited Effectiveness ◽  
Biological Target ◽  
Dual Inhibitors

Diabetes mellitus (DM) represents a group of metabolic disorders that leads to acute and long-term serious complications and is considered a worldwide sanitary emergence. Type 2 diabetes (T2D) represents about 90% of all cases of diabetes, and even if several drugs are actually available for its treatment, in the long term, they show limited effectiveness. Most traditional drugs are designed to act on a specific biological target, but the complexity of the current pathologies has demonstrated that molecules hitting more than one target may be safer and more effective. The purpose of this review is to shed light on the natural compounds known as α-glucosidase and Protein Tyrosine Phosphatase 1B (PTP1B) dual-inhibitors that could be used as lead compounds to generate new multitarget antidiabetic drugs for treatment of T2D.

scholarly journals Prospects for Inhibitors of Protein Tyrosine Phosphatase 1B as Antidiabetic Drugs.

ChemInform ◽  
2004 ◽  
Vol 35 (43) ◽  
Author(s):  
Rob Hooft van Huijsduijnen ◽  
Wolfgang H. B. Sauer ◽  
Agnes Bombrun ◽  
Dominique Swinnen
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Antidiabetic Drugs ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

Prospects for Inhibitors of Protein Tyrosine Phosphatase 1B as Antidiabetic Drugs

2004 ◽  
Vol 47 (17) ◽  
pp. 4142-4146 ◽  
Author(s):  
Rob Hooft van Huijsduijnen ◽  
Wolfgang H. B. Sauer ◽  
Agnes Bombrun ◽  
Dominique Swinnen
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Antidiabetic Drugs ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

Inhibition of Protein Tyrosine Phosphatase 1B by Lutein Derivatives isolated from Mexican Oregano (Lippia graveolens)

2018 ◽  
Vol 17 (3) ◽  
pp. 134-139
Author(s):  
R.M. Perez-Gutierrez
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Inhibitory Activity ◽  
Spectroscopic Data ◽  
Methanol Extract ◽  
Tyrosine Phosphatase ◽  
Positive Control ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Ic50 Value ◽  
Ic50 Values

Methanol extract from Lippia graveolens (Mexican oregano) was studied in order to identify inhibitory bioactives for protein tyrosine phosphatase 1B (PTP1B). Known flavone as lutein (1), and another flavone glycoside such as lutein-7-o-glucoside (2), 6-hydroxy-lutein-7-ohexoside (3) and lutein-7-o-ramnoide (4) were isolated from methanol extract of aerial parts of the Lippia graveolens. All isolates were identified based on extensive spectroscopic data analysis, including UV, IR, NMR, MS and compared with spectroscopic data previously reported. These flavones were evaluated for PTP1B inhibitory activity. Among them, compounds 1 and 3 displayed potential inhibitory activity against PTP1B with IC50 values of 7.01 ± 1.25 μg/ml and 18.4 μg/ml, respectively. In addition, compound 2 and 4 showed moderate inhibitory activity with an IC50 value of 23.8 ± 6.21 and 67.8 ± 5.80 μg/ml respectively. Among the four compounds, luteolin was found to be the most potent PTP1B inhibitor compared to the positive control ursolic acid, with an IC50 value of 8.12 ± 1.06 μg/ml. These results indicate that flavonoids constituents contained in Lippia graveolens can be considered as a natural source for the treatment of type 2 diabetes.

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