دورية أكاديمية

Design, Synthesis, α-Amylase/α-Glucosidase Inhibition Assay, Induced Fit Docking Study of New Hybrid Compounds Containing 4H-Pyrano[2,3-d]pyrimidine, 1H-1,2,3-Triazole and D-Glucose Components.

التفاصيل البيبلوغرافية
العنوان: Design, Synthesis, α-Amylase/α-Glucosidase Inhibition Assay, Induced Fit Docking Study of New Hybrid Compounds Containing 4H-Pyrano[2,3-d]pyrimidine, 1H-1,2,3-Triazole and D-Glucose Components.
المؤلفون: Toan VN; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam.; Institute of New Technology, Academy of Military Science and Technology, Ministry of Defence, 17 Hoang Sam, Cau Giay, Ha Noi, Viet Nam., Thanh ND; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam., Huyen LT; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam., Hanh NT; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam., Hai DS; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam.; Institute of Science and Technology, Ministry of Public Security of Vietnam, 47 Pham Van Dong, Cau Giay, Ha Noi, Viet Nam., Anh HH; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam., Giang NTK; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam.; Institute of Science and Technology, Ministry of Public Security of Vietnam, 47 Pham Van Dong, Cau Giay, Ha Noi, Viet Nam., Van HTK; Faculty of Chemistry, University of Science (Vietnam National University, Hanoi), 19 Le Thanh Tong, Hoan Kiem, Ha Noi, Viet Nam.; Faculty of Chemical Technology, Viet Tri University of Industry, Tien Kien, Lam Thao, Phu Tho, Viet Nam.
المصدر: Chemistry & biodiversity [Chem Biodivers] 2022 Dec; Vol. 19 (12), pp. e202200680. Date of Electronic Publication: 2022 Dec 05.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Verlag Helvetica Chimica Acta Country of Publication: Switzerland NLM ID: 101197449 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1612-1880 (Electronic) Linking ISSN: 16121872 NLM ISO Abbreviation: Chem Biodivers Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Zürich, Switzerland : Hoboken, NJ : Verlag Helvetica Chimica Acta ; Distributed in the USA by Wiley, c2004-
مواضيع طبية MeSH: alpha-Glucosidases*/metabolism , Glucose*, Humans ; Glucosidases/metabolism ; alpha-Amylases/metabolism ; Structure-Activity Relationship ; Amylases/metabolism ; Triazoles/chemistry ; Molecular Docking Simulation ; Glycoside Hydrolase Inhibitors/chemistry ; Pyrimidines/pharmacology ; Pyrimidines/chemistry ; Molecular Structure
مستخلص: In this study, the click chemistry between N-propargyl derivatives of substituted 4H-pyrano[2,3-d]pyrimidines and tetra-O-acetyl-α-d-glucopyranosyl azide carried out under catalytic conditions using catalyst CuI@Montmorillonite and additive N,N-diisopropylethylamine (DIPEA). The yields of obtained hybrid compounds having 4H-pyrano[2,3-d]pyrimidine connected to 1H-1,2,3-triazole rings were about 85-94 %. All these synthesized hybrid compounds were examined for in vitro α-amylase (with IC 50 values in the range of 103.63±1.13 μM to 295.45±1.11 μM) and α-glucosidase (with IC 50 values in the range of 45.63±1.14 μM to 184.52±1.15) inhibitory activity. Amongst this series, ethyl ester 8m showed the best inhibitory activity against α-amylase with IC 50 of 103.63±1.13 μM, while ethyl ester 8t exhibited the highest activity against α-glucosidase with IC 50 of 45.63±1.14 μM. The kinetics of the inhibition of compound 8t showed the competitive α-glucosidase inhibitor property of this compound. Furthermore, the most potent compounds had any cytotoxicity against human normal cells. Induced fit docking and molecular dynamics simulation calculations indicated that the inhibition potential compounds 8m and 8t had the active interactions with the residues in receptors of corresponding tested enzymes. The calculated binding free energy from MM-GBSA approach showed that the major energy components contributed to the active binding of these studied inhibitors, including Coulomb, lipophilic and van der Waals energy. Further, 300 ns MD simulation showed that studied ligand-protein complexes were stable and indicated the structural observations into mode of binding in these complexes.
(© 2022 Wiley-VHCA AG, Zurich, Switzerland.)
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معلومات مُعتمدة: 104.01-2020.01 Vietnam National Foundation for Science and Technology Development (NAFOSTED)
فهرسة مساهمة: Keywords: 4H-pyrano[2,3-d]pyrimidines; hybrid compounds; induced fit docking; sugar azide; type 2 diabetes
المشرفين على المادة: EC 3.2.1.20 (alpha-Glucosidases)
IY9XDZ35W2 (Glucose)
K8CXK5Q32L (pyrimidine)
EC 3.2.1.- (Glucosidases)
EC 3.2.1.1 (alpha-Amylases)
EC 3.2.1.- (Amylases)
0 (Triazoles)
0 (Glycoside Hydrolase Inhibitors)
0 (Pyrimidines)
تواريخ الأحداث: Date Created: 20221121 Date Completed: 20221227 Latest Revision: 20221230
رمز التحديث: 20240628
DOI: 10.1002/cbdv.202200680
PMID: 36408921
قاعدة البيانات: MEDLINE
الوصف
تدمد:1612-1880
DOI:10.1002/cbdv.202200680