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      Tyrosinase Inhibition Antioxidant Effect and Cytotoxicity Studies of the Extracts of Cudrania tricuspidata Fruit Standardized in Chlorogenic Acid

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          Abstract

          In the present study, various extracts of C. tricuspidata fruit were prepared with varying ethanol contents and evaluated for their biomarker and biological properties. The 80% ethanolic extract showed the best tyrosinase inhibitory activity, while the 100% ethanolic extract showed the best total phenolics and flavonoids contents. The HPLC method was applied to analyze the chlorogenic acid in C. tricuspidata fruit extracts. The results suggest that the observed antioxidant and tyrosinase inhibitory activity of C. tricuspidata fruit extract could partially be attributed to the presence of marker compounds in the extract. In this study, we present an analytical method for standardization and optimization of C. tricuspidata fruit preparations. Further investigations are warranted to confirm the in vivo pharmacological activity of C. tricuspidata fruit extract and its active constituents and assess the safe use of the plant for the potential development of the extract as a skin depigmentation agent.

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          Most cited references20

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          Tetrazolium salts and formazan products in Cell Biology: Viability assessment, fluorescence imaging, and labeling perspectives

          For many years various tetrazolium salts and their formazan products have been employed in histochemistry and for assessing cell viability. For the latter application, the most widely used are 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide (MTT), and 5-cyano-2,3-di-(p-tolyl)-tetrazolium chloride (CTC) for viability assays of eukaryotic cells and bacteria, respectively. In these cases, the nicotinamide-adenine-dinucleotide (NAD(P)H) coenzyme and dehydrogenases from metabolically active cells reduce tetrazolium salts to strongly colored and lipophilic formazan products, which are then quantified by absorbance (MTT) or fluorescence (CTC). More recently, certain sulfonated tetrazolium, which give rise to water-soluble formazans, have also proved useful for cytotoxicity assays. We describe several aspects of the application of tetrazolium salts and formazans in biomedical cell biology research, mainly regarding formazan-based colorimetric assays, cellular reduction of MTT, and localization and fluorescence of the MTT formazan in lipidic cell structures. In addition, some pharmacological and labeling perspectives of these compounds are also described.
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            Phenolic composition, antioxidant, anti-wrinkles and tyrosinase inhibitory activities of cocoa pod extract

            Background Cocoa pod is an outer part of cocoa fruits being discarded during cocoa bean processing. Authors found out that data on its usage in literature as cosmetic materials was not recorded in vast. In this study, cocoa pod extract was investigated for its potential as a cosmetic ingredient. Methods Cocoa pod extract (CPE) composition was accomplished using UHPLC. The antioxidant capacity were measured using scavenging assay of 1,2-diphenyl-2-picrylhydrazyl (DPPH), β-carotene bleaching assay (BCB) and ferric reducing antioxidant power (FRAP). Inhibiting effect on skin degradation enzymes was carried out using elastase and collagenase assays. The skin whitening effect of CPE was determined based on mushroom tyrosinase assay and sun screening effect (UV-absorbance at 200-400 nm wavelength). Results LC-MS/MS data showed the presence of carboxylic acid, phenolic acid, fatty acid, flavonoids (flavonol and flavones), stilbenoids and terpenoids in CPE. Results for antioxidant activity exhibited that CPE possessed good antioxidant activity, based on the mechanism of the assays compared with ascorbic acid (AA) and standardized pine bark extract (PBE); DPPH: AA > CPE > PBE; FRAP: PBE > CPE > AA; and BCB: BHT > CPE > PBE. Cocoa pod extract showed better action against elastase and collagenase enzymes in comparison with PBE and AA. Higher inhibition towards tyrosinase enzyme was exhibited by CPE than kojic acid and AA, although lower than PBE. CPE induced proliferation when tested on human fibroblast cell at low concentration. CPE also exhibited a potential as UVB sunscreen despite its low performance as a UVA sunscreen agent. Conclusions Therefore, the CPE has high potential as a cosmetic ingredient due to its anti-wrinkle, skin whitening, and sunscreen effects.
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              Antioxidant and cytotoxic activities of xanthones from Cudrania tricuspidata.

              The new catecholic xanthone, 1,3,7-trihydroxy-4-(1,1-dimethyl-2-propenyl)-5,6-(2,2-dimethylchromeno)-xanthone (1), was isolated from the root bark of Cudrania tricuspidata together with seven known xanthones. The structures were fully characterized by analysis of physical and spectral (UV, IR, mass, and NMR) data. Relationships between the structural characteristics of xanthones and their antioxidant activities (DPPH, superoxide, and hydroxyl radical) were studied. Among the range of catecholic xanthones, 6,7-dihydroxyl xanthones (3-8) exhibited a strong scavenging effect on the DPPH radical. When one of the catecholic hydroxyl groups was protected as in compounds 1 and 2, DPPH radical scavenging activity was markedly decreased (IC(50)>200microM). DPPH activities were consistent with electrochemical response by cyclic voltammetry. Interestingly, compounds (1, 2) which had the weak activities on DPPH, exhibited both potent superoxide and hydroxyl radical scavenging activities. The strong activity on the hydroxyl radical of compounds (1, 2) could be rationalized by their chelating effect with iron (Fe(2+)) due to a redshift of its complex. The catecholic xanthones (3-8), being able to convert quinone methide intermediate, showed potent cytotoxicities against human cancer cell lines (HT-29, HL-60, SK-OV3, AGS, and A549). In particular, compounds 3, 6, and 7 had strong cytotoxic activities against AGS (LD(50)<5microM). DNA fragmentation patterns induced by catecholic xanthones revealed that tumor cell death was due to apoptosis.
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                Author and article information

                Journal
                Molecules
                Molecules
                molecules
                Molecules
                MDPI
                1420-3049
                07 September 2019
                September 2019
                : 24
                : 18
                : 3266
                Affiliations
                [1 ]College of Pharmacy, Mokpo National University, Muan-gun, Jeonnam 58554, Korea
                [2 ]Department of Nursing, Dongshin University, Naju-si, Jeonnam 58245, Korea
                [3 ]Jeollanam-do Forest Resource Research Institute, Naju, Jeonnam 58213, Korea
                [4 ]Department of Biological Sciences, Oakland University, Rochester, MI 48309, USA
                [5 ]Department of Pharmacy, College of Pharmacy, Pusan National University, Busan 46241, Korea
                Author notes
                [* ]Correspondence: s1004jh@ 123456gmail.com (J.-H.S.); sscho@ 123456mokpo.ac.kr (S.-S.C.); Tel.: +82-614502684 (J.-H.S.); +82-614502687 (S.-S.C.)
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0001-7998-4708
                https://orcid.org/0000-0002-0997-5723
                https://orcid.org/0000-0002-4062-4016
                https://orcid.org/0000-0003-1497-0529
                Article
                molecules-24-03266
                10.3390/molecules24183266
                6767289
                31500323
                85528fb5-18e9-4756-81a2-86cd8ba8701d
                © 2019 by the authors.

                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 ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 21 August 2019
                : 06 September 2019
                Categories
                Communication

                c.tricuspidata bureau,hplc,tyrosinase
                c.tricuspidata bureau, hplc, tyrosinase

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