Ursane derivatives isolated from leaves of Hylocereus undatus inhibit glycation at multiple stages.
10.1016/S1875-5364(18)30127-4
- Author:
Pérez-Gutiérrez ROSA MARTHA
1
;
Enriquez-Alvirde SUSANA GABRIELA
2
Author Information
1. Research Laboratory of Natural Products, School of Chemical Engineering and Extractive Industries, National Polytechnic Institute, Av. Instituto Politecnico Nacional S/N, Zacatenco, D.F. CP 07758, Mexico. Electronic address: rmpg@prodigy.net.mx.
2. Research Laboratory of Natural Products, School of Chemical Engineering and Extractive Industries, National Polytechnic Institute, Av. Instituto Politecnico Nacional S/N, Zacatenco, D.F. CP 07758, Mexico.
- Publication Type:Journal Article
- Keywords:
Advanced glycation end product;
Hylocereus undatus;
Triterpenes
- MeSH:
Cactaceae;
chemistry;
Glycation End Products, Advanced;
chemistry;
Glycosylation;
drug effects;
Molecular Structure;
Plant Extracts;
chemistry;
isolation & purification;
pharmacology;
Plant Leaves;
chemistry;
Triterpenes;
chemistry;
isolation & purification;
pharmacology
- From:
Chinese Journal of Natural Medicines (English Ed.)
2018;16(11):856-865
- CountryChina
- Language:English
-
Abstract:
The present study was designed to evaluate the therapeutic potential of bioactive compounds from chloroform extract of the leaves of Hylocereus undatus in the formation of advanced glycation end products (AGEs) in vitro. Bioactivity-guided fractionation of chloroform extract from Hylocereus undatus afforded two novel 12-ursen-type triterpenes, 3β, 16α, 23-trihydroxy-urs-12- en-28-oic acid (1) and 3β, 6β, 19α, 22α-tetrahydroxy-urs-12-en-28-oic acid (2), as well as four known triterpenes 2α, 3β, 23-tetrahydroxy-urs-11-en-28-oic acid (3), 3β-acetoxy-28-hydroxyolean-12-ene (4), 3β, 16α-dihidroxyolean-12-ene (5) and 3β-acetoxy-olean-12-ene (6). Our results revealed that triterpenes 1-3 were able to inhibit the formation of AGEs in all tested assays. The data indicated that the triterpenes had inhibitory activity at the múltiple stages of glycation and that there might be a high potential for decreasing protein oxidation and protein glycation that can enhance glycative stress in diabetic complications.
