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      Antiglycation and Antioxidant Properties of Ficus deltoidea Varieties

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          Abstract

          The present study aimed to evaluate the potential of standardized methanolic extracts from seven Ficus deltoidea varieties in inhibiting the formation of AGEs, protein oxidation, and their antioxidant effects. The antiglycation activity was analyzed based on the inhibition of AGEs, fructosamine, and thiol groups level followed by the inhibition of protein carbonyl formation. The antioxidant activity (DPPH radical scavenging activity and reducing power assay) and total phenolic contents were evaluated. After 28 days of induction, all varieties of Ficus deltoidea extracts significantly restrained the formation of fluorescence AGEs by 4.55–5.14 fold. The extracts also reduced the fructosamine levels by 47.0–86.5%, increased the thiol group levels by 64.3–83.7%, and inhibited the formation of protein carbonyl by 1.36–1.76 fold. DPPH radical scavenging activity showed an IC 50 value of 66.81–288.04  μg/ml and reducing power activity depicted at 0.02–0.24  μg/ml. The extent of phenolic compounds present in the extracts ranged from 70.90 to 299.78 mg·GAE/g. Apart from that, correlation studies between the activities were observed. This study revealed that seven varieties of Ficus deltoidea have the potential to inhibit AGEs formation and possess antioxidant activity that might be attributed to the presence of phenolic compounds.

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          Antioxidative properties of xanthan on the autoxidation of soybean oil in cyclodextrin emulsion

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            Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin.

            The physiological alpha-oxoaldehyde methylglyoxal binds and modifies arginine, lysine, and cysteine residues in proteins. The kinetics and mechanism of these reactions were investigated with N alpha-acetylamino acids and bovine serum albumin at pH 7.4 and 37 degrees C. The reaction of methylglyoxal with N alpha-acetylarginine involved the initial reversible formation of glycosylamine and 4,5-dihydroxy-5-methylimidazolidine derivatives, with further slow irreversible conversion to an imidazolone, N alpha-acetyl-N delta- (5-methyl-4-imidazolon-2-yl)ornithine. The imidazolone was fluorescent with an excitation lambda max value of 320 nm and an emission lambda max value of 398 nm. Methylglyoxal reacted reversibly with N alpha-acetyllysine to form glycosylamine and bisglycosylamine derivatives. Further reaction of these glycosylamines occurred to form brown, fluorescent oligomers that were not characterized. Methylglyoxal reacted rapidly and reversibly with N alpha-acetylcysteine to form the hemithioacetal adduct. The reaction of methylglyoxal with bovine serum albumin (BSA) at pH 7.4 and 37 degrees C involved the reversible and irreversible formation of methylglyoxal-BSA adducts. Irreversible modification of BSA occurred mainly on arginine residues to form imidazolone. The formation of methylglyoxal-modified proteins involves glycoxidation leading to advanced glycation end product-like fluorescence. It is expected to be increased in diabetes mellitus and may be linked to the development of diabetic complications.
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              Inhibition of advanced glycation endproduct formation by foodstuffs.

              The Maillard reaction, which is generally termed nonenzymatic browning or glycation, has been implicated in accelerated aging and diabetic complications in vivo. Although the molecular basis of glycation-induced pathogenesis is not well understood, the following have been noted: (1) protein glycation leads to the formation and accumulation of toxic advanced glycation endproducts (AGEs); (2) AGEs can permanently alter the structure and function of body proteins; and (3) the interaction between AGE-modified proteins and AGE-specific receptors (RAGEs) on the cell surface induces the overproduction of reactive oxygen species (ROSs) and inflammatory mediators, which leads to cellular disorders in biological systems. To date, studies that have examined the contribution of protein glycation to disease-states have primarily focused on the deleterious effects and related mechanisms of these glycotoxins. However, it remains unknown whether phytochemicals exert protective effects against glycotoxin-induced damage. Thus, the development and investigation of AGE inhibitors, especially the natural anti-AGE agents without adverse effects, may provide a therapeutic approach for delaying and preventing premature aging and diabetic complications. In this review, we provide an outline of anti-glycation properties of foodstuffs and/or their active components, and discuss their mechanisms of action.
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                Author and article information

                Contributors
                Journal
                Evid Based Complement Alternat Med
                Evid Based Complement Alternat Med
                ECAM
                Evidence-based Complementary and Alternative Medicine : eCAM
                Hindawi
                1741-427X
                1741-4288
                2020
                7 August 2020
                7 August 2020
                : 2020
                : 6374632
                Affiliations
                1Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Seri Kembangan, Selangor, Malaysia
                2Department of Chemical Engineering Technology, Faculty of Engineering Technology, Universiti Malaysia Perlis, 02100 Sungai Chuchuh, Padang Besar, Perlis, Malaysia
                3Medical Technology Division, Malaysian Nuclear Agency, Bangi 43000, Kajang, Selangor, Malaysia
                4Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Seri Kembangan, Selangor, Malaysia
                Author notes

                Academic Editor: George B. Lenon

                Author information
                https://orcid.org/0000-0002-3140-832X
                https://orcid.org/0000-0001-8157-0635
                https://orcid.org/0000-0003-4835-4687
                https://orcid.org/0000-0002-2475-7628
                Article
                10.1155/2020/6374632
                7428875
                32831872
                234ee2bd-e0dd-422e-91c6-494baec3bc2c
                Copyright © 2020 Nur Sumirah Mohd Dom et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 24 April 2020
                : 24 June 2020
                : 17 July 2020
                Funding
                Funded by: Malaysian Government
                Award ID: NH1014D036
                Categories
                Research Article

                Complementary & Alternative medicine
                Complementary & Alternative medicine

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