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1.
Int J Biol Macromol ; 102: 960-969, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28455256

RESUMO

The enzyme α-glucosidase is a good drug target for the treatment of diabetes mellitus. Four minor flavonoids (1-4) from roots of Sophora flavescens showed the inhibitory activity, with IC50 values ranging from 11.0±0.3 to 50.6±1.3µM, toward α-glucosidase. An enzyme kinetics analysis of them revealed that the compounds 1 and 4 were non-competitive, and compounds 2 and 3 were un-competitive inhibitors. For molecular docking, 3-dimensional structure of α-glucosidase was built by homology modeling. As the result, four compounds 1-4 were confirmed to interact into common binding site of α-glucosidase. In addition, all of the four prenylated and lavandulyl compounds (1-4) were abundant in an ethyl acetate fraction separated from a methanol extract, and the potential inhibitor (3) was extracted best using tetrahydrofuran.


Assuntos
Simulação por Computador , Extratos Vegetais/farmacologia , Raízes de Plantas/química , Prenilação , Sophora/química , Terpenos/química , alfa-Glucosidases/metabolismo , Sequência de Aminoácidos , Inibidores de Glicosídeo Hidrolases/química , Inibidores de Glicosídeo Hidrolases/metabolismo , Inibidores de Glicosídeo Hidrolases/farmacologia , Simulação de Acoplamento Molecular , Extratos Vegetais/química , Extratos Vegetais/metabolismo , Conformação Proteica , alfa-Glucosidases/química
2.
J Enzyme Inhib Med Chem ; 32(1): 78-83, 2017 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-27778516

RESUMO

A new compound, 9-dihydroxyl-2'-O-(Z)-cinnamoyl-7-methoxy-aloesin (1), and eight known compounds (2-9) were isolated from Aloe vera. Their structures were elucidated using 1D/2D nuclear magnetic resonance and mass spectra. Compound 9 exhibited reversible competitive inhibitory activity against the enzyme tyrosinase, with an IC50 value of 9.8 ± 0.9 µM. A molecular simulation revealed that compound 9 interacts via hydrogen bonding with residues His244, Thr261, and Val283 of tyrosinase. Additionally, compounds 3 and 7 were shown by half-leaf assays to exhibit inhibitory activity towards Pepper mild mottle virus.


Assuntos
Aloe/química , Antivirais/farmacologia , Inibidores Enzimáticos/farmacologia , Monofenol Mono-Oxigenase/antagonistas & inibidores , Extratos Vegetais/farmacologia , Antivirais/química , Espectroscopia de Ressonância Magnética Nuclear de Carbono-13 , Inibidores Enzimáticos/química , Simulação de Acoplamento Molecular , Vírus de Plantas/efeitos dos fármacos , Espectroscopia de Prótons por Ressonância Magnética , Espectrometria de Massas por Ionização por Electrospray
3.
J Microbiol Biotechnol ; 26(12): 2138-2140, 2016 Dec 28.
Artigo em Inglês | MEDLINE | ID: mdl-27586528

RESUMO

The goal of this study was to identify a source of natural plant compounds with inhibitory activity against pepper mild mottle virus (PMMoV). We showed, using a half-leaf assay, that murrayafoline-A (1) and isomahanine (2) isolated from the aerial parts of Glycosmis stenocarpa have inhibitory activity against PMMoV through curative, inactivation, and protection effects. Using a leaf-disk assay, we confirmed that 2 inhibited virus replication in Nicotiana benthamiana. Using electron microscopy, we found that a mixture of the virus with 2 resulted in damage to the rod-shaped virus.


Assuntos
Antivirais/farmacologia , Extratos Vegetais/farmacologia , Rutaceae/química , Tobamovirus/efeitos dos fármacos , Doenças das Plantas/virologia , Nicotiana/virologia , Tobamovirus/fisiologia , Replicação Viral/efeitos dos fármacos
4.
Molecules ; 20(12): 21405-14, 2015 Dec 02.
Artigo em Inglês | MEDLINE | ID: mdl-26633335

RESUMO

Selaginellin derivatives 1-3 isolated from Selaginella tamariscina were evaluated for their inhibition of soluble epoxide hydrolase (sEH) to demonstrate their potential for the treatment of cardiovascular disease. All selaginellin derivatives (1-3) inhibited sEH enzymatic activity and PHOME hydrolysis, in a dose-dependent manner, with IC50 values of 3.1 ± 0.1, 8.2 ± 2.2, and 4.2 ± 0.2 µM, respectively. We further determined that the derivatives function as non-competitive inhibitors. Moreover, the predicted that binding sites and interaction between 1-3 and sEH were solved by docking simulations. According to quantitative analysis, 1-3 were confirmed to have high content in the roots of S. tamariscina; among them, selaginellin 3 exhibited the highest content of 189.3 ± 0.0 µg/g.


Assuntos
Cicloexanonas/farmacologia , Inibidores Enzimáticos/farmacologia , Epóxido Hidrolases/antagonistas & inibidores , Extratos Vegetais/farmacologia , Selaginellaceae/química , Cicloexanonas/química , Inibidores Enzimáticos/química , Humanos , Estrutura Molecular
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