Steroidal saponins from Trillium govanianum as α-amylase, α-glucosidase, and dipeptidyl peptidase IV inhibitory agents.


Journal

The Journal of pharmacy and pharmacology
ISSN: 2042-7158
Titre abrégé: J Pharm Pharmacol
Pays: England
ID NLM: 0376363

Informations de publication

Date de publication:
08 Mar 2021
Historique:
received: 31 05 2020
accepted: 27 10 2020
entrez: 1 4 2021
pubmed: 2 4 2021
medline: 9 11 2021
Statut: ppublish

Résumé

To provide the scientific basis for the utility of rhizome of Trillium govanianum as nutraceutical supplements in managing physiological glycemic levels. The in vitro enzyme inhibitory activity of the extract, fractions, and the isolated steroidal saponins from the rhizome part of T. govanianum was carried out against α-amylase, α-glucosidase, and dipeptidyl peptidase IV. The molecular interactions, binding score, and pharmacokinetic parameters (absorption, distribution metabolism, and excretion) of steroidal saponins were analyzed by the Schrodinger molecular docking software. Current study explained that the extract, fractions, and isolated steroidal saponins from T. govanianum possess good α-amylase and α-glucosidase inhibitory activity while moderate dipeptidyl peptidase IV inhibitory activity. Moreover, in vitro results revealed that borassoside E (IC50 7.15 ± 1.78 μM), protodioscin (IC50 6.72 ± 0.04 μM), and diosgenin (IC50 12.75 ± 2.70 μM) are most effective in inhibiting the activity of α-amylase, α-glucosidase, and dipeptidyl peptidase IV, respectively. Current in silico and in vitro studies established an association between the steroidal saponins from T. govanianum and their molecular interactions with α-amylase, α-glucosidase, and dipeptidyl peptidase IV. The results of this investigation suggest that fractions and steroidal saponins from T. govanianum exhibit good antidiabetic activity which could be used as nutraceutical supplements for the management of systemic glucose level.

Identifiants

pubmed: 33793831
pii: 6102453
doi: 10.1093/jpp/rgaa038
doi:

Substances chimiques

Dipeptidyl-Peptidase IV Inhibitors 0
Enzyme Inhibitors 0
Glycoside Hydrolase Inhibitors 0
Hypoglycemic Agents 0
Plant Extracts 0
Saponins 0
alpha-Amylases EC 3.2.1.1
alpha-Glucosidases EC 3.2.1.20
Dipeptidyl Peptidase 4 EC 3.4.14.5

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

487-495

Informations de copyright

© The Author(s) 2021. Published by Oxford University Press on behalf of Royal Pharmaceutical Society. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Auteurs

Patil Shivprasad Suresh (PS)

Chemical Technology Division, CSIR-IHBT, Palampur, India.
Food and Nutraceuticals Division, CSIR-IHBT, Palampur, India.
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, U.P., India.

Prithvi Pal Singh (PP)

Chemical Technology Division, CSIR-IHBT, Palampur, India.
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, U.P., India.

Yogendra S Padwad (YS)

Food and Nutraceuticals Division, CSIR-IHBT, Palampur, India.
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, U.P., India.

Upendra Sharma (U)

Chemical Technology Division, CSIR-IHBT, Palampur, India.
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, U.P., India.

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Classifications MeSH