Cargando…
Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies
Diabetes mellitus is characterized by chronic hyperglycemia that promotes ROS formation, causing severe oxidative stress. Furthermore, prolonged hyperglycemia leads to glycation reactions with formation of AGEs that contribute to a chronic inflammatory state. This research aims to evaluate the inhib...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8777799/ https://www.ncbi.nlm.nih.gov/pubmed/35056861 http://dx.doi.org/10.3390/molecules27020547 |
_version_ | 1784637153898135552 |
---|---|
author | Djeujo, Francine Medjiofack Francesconi, Valeria Gonella, Maddalena Ragazzi, Eugenio Tonelli, Michele Froldi, Guglielmina |
author_facet | Djeujo, Francine Medjiofack Francesconi, Valeria Gonella, Maddalena Ragazzi, Eugenio Tonelli, Michele Froldi, Guglielmina |
author_sort | Djeujo, Francine Medjiofack |
collection | PubMed |
description | Diabetes mellitus is characterized by chronic hyperglycemia that promotes ROS formation, causing severe oxidative stress. Furthermore, prolonged hyperglycemia leads to glycation reactions with formation of AGEs that contribute to a chronic inflammatory state. This research aims to evaluate the inhibitory activity of α-mangostin and four synthetic xanthenone derivatives against glycation and oxidative processes and on α-glucosidase, an intestinal hydrolase that catalyzes the cleavage of oligosaccharides into glucose molecules, promoting the postprandial glycemic peak. Antiglycation activity was evaluated using the BSA assay, while antioxidant capacity was detected with the ORAC assay. The inhibition of α-glucosidase activity was studied with multispectroscopic methods along with inhibitory kinetic analysis. α-Mangostin and synthetic compounds at 25 µM reduced the production of AGEs, whereas the α-glucosidase activity was inhibited only by the natural compound. α-Mangostin decreased enzymatic activity in a concentration-dependent manner in the micromolar range by a reversible mixed-type antagonism. Circular dichroism revealed a rearrangement of the secondary structure of α-glucosidase with an increase in the contents of α-helix and random coils and a decrease in β-sheet and β-turn components. The data highlighted the anti-α-glucosidase activity of α-mangostin together with its protective effects on protein glycation and oxidation damage. |
format | Online Article Text |
id | pubmed-8777799 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87777992022-01-22 Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies Djeujo, Francine Medjiofack Francesconi, Valeria Gonella, Maddalena Ragazzi, Eugenio Tonelli, Michele Froldi, Guglielmina Molecules Article Diabetes mellitus is characterized by chronic hyperglycemia that promotes ROS formation, causing severe oxidative stress. Furthermore, prolonged hyperglycemia leads to glycation reactions with formation of AGEs that contribute to a chronic inflammatory state. This research aims to evaluate the inhibitory activity of α-mangostin and four synthetic xanthenone derivatives against glycation and oxidative processes and on α-glucosidase, an intestinal hydrolase that catalyzes the cleavage of oligosaccharides into glucose molecules, promoting the postprandial glycemic peak. Antiglycation activity was evaluated using the BSA assay, while antioxidant capacity was detected with the ORAC assay. The inhibition of α-glucosidase activity was studied with multispectroscopic methods along with inhibitory kinetic analysis. α-Mangostin and synthetic compounds at 25 µM reduced the production of AGEs, whereas the α-glucosidase activity was inhibited only by the natural compound. α-Mangostin decreased enzymatic activity in a concentration-dependent manner in the micromolar range by a reversible mixed-type antagonism. Circular dichroism revealed a rearrangement of the secondary structure of α-glucosidase with an increase in the contents of α-helix and random coils and a decrease in β-sheet and β-turn components. The data highlighted the anti-α-glucosidase activity of α-mangostin together with its protective effects on protein glycation and oxidation damage. MDPI 2022-01-15 /pmc/articles/PMC8777799/ /pubmed/35056861 http://dx.doi.org/10.3390/molecules27020547 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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/). |
spellingShingle | Article Djeujo, Francine Medjiofack Francesconi, Valeria Gonella, Maddalena Ragazzi, Eugenio Tonelli, Michele Froldi, Guglielmina Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title | Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title_full | Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title_fullStr | Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title_full_unstemmed | Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title_short | Anti-α-Glucosidase and Antiglycation Activities of α-Mangostin and New Xanthenone Derivatives: Enzymatic Kinetics and Mechanistic Insights through In Vitro Studies |
title_sort | anti-α-glucosidase and antiglycation activities of α-mangostin and new xanthenone derivatives: enzymatic kinetics and mechanistic insights through in vitro studies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8777799/ https://www.ncbi.nlm.nih.gov/pubmed/35056861 http://dx.doi.org/10.3390/molecules27020547 |
work_keys_str_mv | AT djeujofrancinemedjiofack antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies AT francesconivaleria antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies AT gonellamaddalena antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies AT ragazzieugenio antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies AT tonellimichele antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies AT froldiguglielmina antiaglucosidaseandantiglycationactivitiesofamangostinandnewxanthenonederivativesenzymatickineticsandmechanisticinsightsthroughinvitrostudies |