Journal Article Epublish
PubMed: 38475490 DOI: 10.3390/plants13050644
Identification of Hypoglycemic Glycolipids from by Affinity-Directed Fractionation, In Vitro, In Silico and Dynamic Light Scattering Analysis.
Plants (Basel) 13(5)
Authors: Daniel Rosas-Ramírez, Roberto Arreguín-Espinosa, Sonia Escandón-Rivera, Adolfo Andrade-Cetto, Gerardo Mata-Torres, Ricardo Pérez-Solís
Affiliations
- Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, Av. Universidad 3000, Circuito Exterior s/n, Coyoacán, Ciudad Universitaria, Mexico City 04510, Mexico.
- Departamento de Biología Celular, Facultad de Ciencias, Universidad Nacional Autónoma de México, Av. Universidad 3000, Circuito Exterior s/n, Coyoacán, Ciudad Universitaria, Mexico City 04510, Mexico.
- Departamento de Ingenieria Mecatrónica, Tecnológico Nacional de México, Instituto Tecnológico Superior de Atlixco, Heliotropo 1201, Unidad 8 Norte Nueva Xalpatlaco, Vista Hermosa, Atlixco 74218, Mexico.
Abstract
In the pursuit of identifying the novel resin glycoside modulators glucose-6-phosphatase and -glucosidase enzymes, associated with blood sugar regulation, methanol-soluble extracts from the flowers of (cazahuate, Nahuatl), renowned for its abundance of glycolipids, were employed. The methanol-soluble extracts were fractionated by applying the affinity-directed method with glucose-6-phosphatase enzymes from a rat's liver and -glucosidase enzymes from its intestines. Mass spectrometry and nuclear magnetic resonance were employed to identify the high-affinity compound as a free ligand following the release from the enzymatic complex. Gel permeation through a spin size-exclusion column allowed the separated high-affinity molecules to bind to glucose-6-phosphatase and -glucosidase enzymes in solution, which led to the identification of some previously reported resin glycosides in the flowers of cazahuate, where a glycolipid mainly structurally related to murucoidin XIV was observed. In vitro studies demonstrated the modulating properties of resin glycosides on the glucose-6-phosphatase enzyme. Dynamic light scattering revealed conformational variations induced by resin glycosides on -glucosidase enzyme, causing them to become more compact, akin to observations with the positive control, acarbose. These findings suggest that resin glycosides may serve as a potential source for phytotherapeutic agents with antihyperglycemic properties.
MeSH
Glycolipids, Glucosidases, Hypoglycemic Agents, Enzymes, Methanol, Glycosides, Glucose-6-Phosphatase