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On the Inhibitability of Natural Products Isolated from Tetradium ruticarpum towards Tyrosine Phosphatase 1B (PTP1B) and α-Glucosidase (3W37): An In Vitro and In Silico Study

Molecules (Basel, Switzerland), 2021-06, Vol.26 (12), p.3691 [Peer Reviewed Journal]

2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2021 by the authors. 2021 ;ISSN: 1420-3049 ;EISSN: 1420-3049 ;DOI: 10.3390/molecules26123691 ;PMID: 34204232

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Title:
On the Inhibitability of Natural Products Isolated from Tetradium ruticarpum towards Tyrosine Phosphatase 1B (PTP1B) and α-Glucosidase (3W37): An In Vitro and In Silico Study
Author: To, Dao-Cuong ; Bui, Thanh Q ; Nhung, Nguyen Thi Ai ; Tran, Quoc-Toan ; Do, Thi-Thuy ; Tran, Manh-Hung ; Hien, Phan-Phuoc ; Ngu, Truong-Nhan ; Quy, Phan-Tu ; Nguyen, The-Hung ; Nguyen, Huu-Tho ; Nguyen, Tien-Dung ; Nguyen, Phi-Hung
Subjects: alpha-Glucosidases - drug effects ; alpha-Glucosidases - metabolism ; Biological Products - chemistry ; Biological Products - pharmacology ; Carbon ; Chinese medicine ; Computer applications ; Density functional theory ; Diabetes ; Diabetes mellitus ; Enzymatic activity ; Enzyme Inhibitors - pharmacology ; Enzymes ; Evodia - metabolism ; Glucose ; Glucosidase ; Glycoside Hydrolase Inhibitors - chemistry ; Herbal medicine ; Homeostasis ; Hyperglycemia ; Inhibitors ; Insulin resistance ; Kinases ; Ligands ; Molecular docking ; Molecular Docking Simulation ; Natural products ; Obesity ; Phosphatase ; Plant Extracts - chemistry ; Plant Extracts - pharmacology ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - drug effects ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism ; Protein-tyrosine-phosphatase ; Proteins ; Simulation ; Structure-Activity Relationship ; Tetradium ruticarpum ; Tyrosine ; tyrosine phosphatase 1B (PTP1B) ; α-Glucosidase ; α-glucosidase (3W37)
Is Part Of: Molecules (Basel, Switzerland), 2021-06, Vol.26 (12), p.3691
Description: Folk experiences suggest natural products in can be effective inhibitors towards diabetes-related enzymes. The compounds were experimentally isolated, structurally elucidated, and tested in vitro for their inhibition effects on tyrosine phosphatase 1B (PTP1B) and α-glucosidase (3W37). Density functional theory and molecular docking techniques were utilized as computational methods to predict the stability of the ligands and simulate interaction between the studied inhibitory agents and the targeted proteins. Structural elucidation identifies two natural products: 2-heptyl-1-methylquinolin-4-one ( ) and 3-[4-(4-methylhydroxy-2-butenyloxy)-phenyl]-2-propenol ( ). In vitro study shows that the compounds ( and ) possess high potentiality for the inhibition of PTP1B (IC values of 24.3 ± 0.8, and 47.7 ± 1.1 μM) and α-glucosidase (IC values of 92.1 ± 0.8, and 167.4 ± 0.4 μM). DS values and the number of interactions obtained from docking simulation highly correlate with the experimental results yielded. Furthermore, in-depth analyses of the structure-activity relationship suggest significant contributions of amino acids Arg254 and Arg676 to the conformational distortion of PTP1B and 3W37 structures overall, thus leading to the deterioration of their enzymatic activity observed in assay-based experiments. This study encourages further investigations either to develop appropriate alternatives for diabetes treatment or to verify the role of amino acids Arg254 and Arg676.
Publisher: Switzerland: MDPI AG
Language: English
Identifier: ISSN: 1420-3049
EISSN: 1420-3049
DOI: 10.3390/molecules26123691
PMID: 34204232
Source: Open Access: PubMed Central
Geneva Foundation Free Medical Journals at publisher websites
MEDLINE
Alma/SFX Local Collection
ProQuest Central
DOAJ Directory of Open Access Journals

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On the Inhibitability of Natural Products Isolated from Tetradium ruticarpum towards Tyrosine Phosphatase 1B (PTP1B) and α-Glucosidase (3W37): An In Vitro and In Silico Study

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