B procyanidins of Annona crassiflora fruit peel inhibited glycation, lipid peroxidation and protein-bound carbonyls, with protective effects on glycated catalase

Abstract

Advanced glycation end-products (AGEs) have been reported as results of increased oxidative stress. Consequently, the search for new antioxidant and anti-glycating agents is under intense investigation. Plant-derived procyanidins have previously demonstrated anti-glycation properties. Thus, this study aimed to isolate procyanidins from Annona crassiflora fruit peel, a species from the Brazilian Savanna, and investigate their antioxidant and anti-glycation effects. Free radical scavenging and quenching properties, formation of reactive oxygen species (ROS), AGEs, protein carbonyl and thiol groups, lipid peroxidation, crosslinked AGEs, as well as glycated catalase activity, were analyzed. In addition, in silico assessment of absorption, distribution, metabolism, excretion and toxicity was carried out. The procyanidins-enriched fraction, named here as F7, showed high antioxidant and anti-glycation capacities, with inhibitory activities against lipid peroxidation, and AGEs and ROS formation. In addition, there were reductions in AGEs-induced crosslinks and protein carbonyls and protective effects against oxidation of thiol groups and glycated-catalase. ADMET predictions of F7 showed favorable absorption and distribution, with no hepatotoxicity or mutagenicity. Together, our results support the anti-glycation activities of the procyanidins-enriched fraction from A. crassiflora, and suggest that these effects are triggered, at least in part, by scavenging free radical and dicarbonyls intermediates.

In vitro antioxidant and antidiabetic activity of essential oils encapsulated in gelatin‐pectin particles against sugar, lipid and protein oxidation and amylase and glucosidase activity

“…ODEO, TAEO, TKEO, and ZMEO diminished protein glycosylation in the presence of glyceraldehyde at 145–170 µg/ml similar to aminoguanidine (Table 3). Protein glycosylation is the reaction between reducing sugars (glucose, fructose, and glyceraldehyde) and amine groups of amino acid side chains leading to the formation of amadori products and over a long time produces glycosylation products (Justino et al., 2019). Glycosylation of proteins and enzymes causes the progression of pathological disorders known as atherosclerosis, diabetes, neurodegenerative and renal diseases.…”

Protective Effects of Swertiamarin against Methylglyoxal induced Damage and its Role in Preventing Diabetic Nephropathy by Improving Oxidative Stress in Rat Kidney Epithelial (NRK-52E) Cells

“…Fructose leads to the formation of AGEs and ROS by promoting the glycation of proteins and lipids, also aided by MG which is a dicarbonyl fomed during glycolytic pathway for glucose metabolism [43]. Hence, preventing the glycation induced by fructose and MG could be one of the prime strategies to inhibit the formation of AGEs and prevent the diabetes related complications [44].…”

Procyanidins: From Agro-Industrial Waste to Food as Bioactive Molecules

“…A recent finding in laurel wood extracts demonstrated that B-type dimer and A type trimer procyanidins exhibited antimicrobial and antibiofilm activity [ 82 ]. Procyanidin of Annona crassiflora fruit peel show antiglycation capacities [ 83 ]. From Vaccinium meridionale Swartz pomace was obtained A-type procyanidin, demonstrating its effectiveness in the control of pathogenic bacteria [ 84 ].…”