Displaying publications 1 - 20 of 31 in total

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  1. Review on pharmacological activities of Cinnamomum subavenium
    Lee CH, Kuo CN, Chen HL, Chen CY
    Nat Prod Res, 2013;27(11):988-91.
    PMID: 22691063 DOI: 10.1080/14786419.2012.695369
    This review describes the morphological, phytochemical and pharmacological properties of Cinnamomum subavenium (Lauraceae). The plant grows wild in southern Mainland China, Burma, Cambodia, Taiwan, Malaysia and Indonesia. This plant is recorded as having long been used to treat carcinomatous swelling, stomach ache, chest pain, abdominal pain, hernia, diarrhoea, rheumatism, nausea and vomiting. This article enumerates an overview of phytochemical and pharmacological aspects that is useful to researchers for further exploration for the necessary development of this potential herb.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors
  2. Fulltext Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities
    Bahari AN, Saari N, Salim N, Ashari SE
    Molecules, 2020 Jun 08;25(11).
    PMID: 32521731 DOI: 10.3390/molecules25112663
    Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate skin aging. In the present study, pH, reaction temperature, reaction time and enzyme/substrate ratio (E/S) have been identified as the parameters in the papain enzymatic hydrolysis of A. lecanora. The degree of hydrolysis (DH) with antioxidant activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric-reducing antioxidant power (FRAP) assays were used as the responses in the optimization. Analysis of variance (ANOVA), normal plot of residuals and 3D contour plots were evaluated to study the effects and interactions between parameters. The best conditions selected from the optimization were at pH 5.00, 70 °C of reaction temperature, 9 h of hydrolysis time and 1.00% enzyme/substrate (E/S) ratio, with the hydrolysates having 51.90% of DH, 42.70% of DPPH activity and 109.90 Fe2+μg/mL of FRAP activity. The A. lecanora hydrolysates (ALH) showed a high amount of hydrophobic amino acids (286.40 mg/g sample) that might be responsible for antioxidant and antityrosinase activities. Scanning electron microscopy (SEM) image of ALH shows smooth structures with pores. Antityrosinase activity of ALH exhibited inhibition of 31.50% for L-tyrosine substrate and 25.40% for L-DOPA substrate. This condition suggests that the optimized ALH acquired has the potential to be used as a bioactive ingredient for cosmeceutical applications.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  3. Fulltext Carvacrol derivatives as mushroom tyrosinase inhibitors; synthesis, kinetics mechanism and molecular docking studies
    Ashraf Z, Rafiq M, Nadeem H, Hassan M, Afzal S, Waseem M, et al.
    PLoS One, 2017;12(5):e0178069.
    PMID: 28542395 DOI: 10.1371/journal.pone.0178069
    The present work describesthe development of highly potent mushroom tyrosinase inhibitor better than the standard kojic acid. Carvacrol derivatives 4a-f and 6a-d having substituted benzoic acid and cinnamic acidresidues were synthesized with the aim to possess potent tyrosinase inhibitory activity.The structures of the synthesized compounds were ascertained by their spectroscopic data (FTIR, 1HNMR, 13CNMR and Mass Spectroscopy).Mushroom tyrosinase inhibitory activity of synthesized compounds was determined and it was found that one of the derivative 6c possess higher activity (IC50 0.0167μM) than standard kojic acid (IC50 16.69μM). The derivatives 4c and 6b also showed good tyrosinase inhibitory activity with (IC50 16.69μM) and (IC50 16.69μM) respectively.Lineweaver-Burk and Dixon plots were used for the determination of kinetic mechanism of the compounds 4c and 6b and 6c. The kinetic analysis revealed that compounds 4c and 6b showed mixed-type inhibition while 6c is a non-competitive inhibitor having Ki values19 μM, 10 μM, and 0.05 μMrespectively. The enzyme inhibitory kinetics further showed thatcompounds 6b and 6c formed irreversible enzyme inhibitor complex while 4c bind reversibly with mushroom tyrosinase.The docking studies showed that compound 6c have maximum binding affinity against mushroom tyrosinase (PDBID: 2Y9X) with binding energy value (-7.90 kcal/mol) as compared to others.The 2-hydroxy group in compound 6c interacts with amino acid HIS85 which is present in active binding site. The wet lab results are in good agreement with the dry lab findings.Based upon our investigation we may propose that the compound 6c is promising candidate for the development of safe cosmetic agent.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  4. Antioxidative, tyrosinase inhibiting and antibacterial activities of leaf extracts from medicinal ferns
    Lai HY, Lim YY, Tan SP
    Biosci Biotechnol Biochem, 2009 Jun;73(6):1362-6.
    PMID: 19502733
    Leaf extracts of five medicinal ferns, Acrostichum aureum L. (Pteridaceae), Asplenium nidus L. (Aspleniaceae), Blechnum orientale L. (Blechnaceae), Cibotium barometz (L.) J. Sm. (Cyatheaceae) and Dicranopteris linearis (Burm.) underwood var. linearis (Gleicheniaceae), were investigated for their total phenolic content (TPC), and antioxidative, tyrosinase inhibiting and antibacterial activities. The antioxidative activity was measured by assays for radical scavenging against 1,1-diphenyl-2-picrylhydrazyl (DPPH), ferric ion reducing power (FRP), beta-carotene bleaching (BCB) and ferrous ion chelating (FIC). The results revealed B. orientale to possess the highest amount of total polyphenols and strongest potential as a natural antioxidative, tyrosinase inhibiting and antibacterial agent as demonstrated by its strong activities in all related bioassays. The other ferns with antioxidative potential were C. barometz and D. linearis. Except for A. aureum, all ferns showed antibacterial activity which may justify their usage in traditional medicines.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  5. Ultrasound mediated efficient synthesis of new 4-oxoquinazolin-3(4H)-yl)furan-2-carboxamides as potent tyrosinase inhibitors: Mechanistic approach through chemoinformatics and molecular docking studies
    Dige NC, Mahajan PG, Raza H, Hassan M, Vanjare BD, Hong H, et al.
    Bioorg Chem, 2019 11;92:103201.
    PMID: 31445195 DOI: 10.1016/j.bioorg.2019.103201
    We have carried out the synthesis of new 4-oxoquinazolin-3(4H)-yl)furan-2-carboxamide derivatives by the reaction between isatoic anhydride, 2-furoic hydrazide and substituted salicylaldehydes in ethanol: water (5:5 v/v) solvent system using p-TSA as a catalyst under ultrasound irradiation at room temperature. The structures of newly synthesized compounds were confirmed through spectral techniques such as IR, 1H NMR, 13C NMR, and LCMS. The important features of this protocol include simple and easy workup procedure, reaction carried out at ambient temperature, use of ultrasound and high yield of oxoquinazolin-3(4H)-yl)furan-2-carboxamides in short reaction time. The synthesized compounds 4a-4j were screened against tyrosinase enzyme and all these compounds found to be potent inhibitors with much lower IC50 value of 0.028 ± 0.016 to 1.775 ± 0.947 µM than the standard kojic acid (16.832 ± 1.162 µM). The kinetics mechanism for compound 4e was analyzed by Lineweaver-Burk plots which revealed that compound inhibited tyrosinase non-competitively by forming an enzyme-inhibitor complex. Along with this all the synthesized compounds (4a-4j) were scanned for their DPPH free radical scavenging ability. The outputs received through in vitro and in silico analysis are coherent to the each other with good binding energy values (kcal/mol) posed by synthesized ligands.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  6. Extraction, anti-tyrosinase, and antioxidant activities of the collagen hydrolysate derived from Rhopilema hispidum
    Ab Aziz NA, Salim N, Zarei M, Saari N, Yusoff FM
    Prep Biochem Biotechnol, 2021;51(1):44-53.
    PMID: 32701046 DOI: 10.1080/10826068.2020.1789991
    The study was conducted to determine anti-tyrosinase and antioxidant activities of the extracted collagen hydrolysate (CH) derived from Malaysian jellyfish, Rhopilema hispidum. Collagen was extracted using 1:1 (w:v) 0.1 M NaOH solution at temperature 25 °C for 48 hr followed by treatment of 1:2 (w:v) distilled water for another 24 hr and freeze-dried. The extracted collagen was hydrolyzed using papain at optimum temperature, pH and enzyme/substrate ratio [E/S] of 60 °C, 7.0 and 1:50, respectively. CH was found to exhibit tyrosinase inhibitory activity, DPPH radical scavenging and metal ion-chelating assays up to 64, 28, and 83%, respectively, after 8 hr of hydrolysis process. The molecular weight of CH was found <10 kDa consisting of mainly Gly (19.219%), Glu (10.428%), and Arg (8.848%). The UV-visible spectrum analysis showed a major and minor peak at 218 and 276 nm, accordingly. The FTIR spectroscopy confirmed the amide groups in CH. The SEM images demonstrated spongy and porous structure of CH. In the cytotoxicity study, CH has no cytotoxicity against mouse embryonic 3T3 fibroblast cell line with IC50 value >500 µg/ml. Results revealed that the CH generated from this study has a potential to be developed as active ingredient in cosmeceutical application.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  7. Fulltext Novel biphenyl ester derivatives as tyrosinase inhibitors: Synthesis, crystallographic, spectral analysis and molecular docking studies
    Kwong HC, Chidan Kumar CS, Mah SH, Chia TS, Quah CK, Loh ZH, et al.
    PLoS One, 2017;12(2):e0170117.
    PMID: 28241010 DOI: 10.1371/journal.pone.0170117
    Biphenyl-based compounds are clinically important for the treatments of hypertension and inflammatory, while many more are under development for pharmaceutical uses. In the present study, a series of 2-([1,1'-biphenyl]-4-yl)-2-oxoethyl benzoates, 2(a-q), and 2-([1,1'-biphenyl]-4-yl)-2-oxoethyl pyridinecarboxylate, 2(r-s) were synthesized by reacting 1-([1,1'-biphenyl]-4-yl)-2-bromoethan-1-one with various carboxylic acids using potassium carbonate in dimethylformamide at ambient temperature. Single-crystal X-ray diffraction studies revealed a more closely packed crystal structure can be produced by introduction of biphenyl moiety. Five of the compounds among the reported series exhibited significant anti-tyrosinase activities, in which 2p, 2r and 2s displayed good inhibitions which are comparable to standard inhibitor kojic acid at concentrations of 100 and 250 μg/mL. The inhibitory effects of these active compounds were further confirmed by computational molecular docking studies and the results revealed the primary binding site is active-site entrance instead of inner copper binding site which acted as the secondary binding site.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  8. Fulltext Bioactive compounds, antioxidant, xanthine oxidase inhibitory, tyrosinase inhibitory and anti-inflammatory activities of selected agro-industrial by-products
    Oskoueian E, Abdullah N, Hendra R, Karimi E
    Int J Mol Sci, 2011;12(12):8610-25.
    PMID: 22272095 DOI: 10.3390/ijms12128610
    Evaluation of abundantly available agro-industrial by-products for their bioactive compounds and biological activities is beneficial in particular for the food and pharmaceutical industries. In this study, rapeseed meal, cottonseed meal and soybean meal were investigated for the presence of bioactive compounds and antioxidant, anti-inflammatory, xanthine oxidase and tyrosinase inhibitory activities. Methanolic extracts of rapeseed meal showed significantly (P < 0.01) higher phenolics and flavonoids contents; and significantly (P < 0.01) higher DPPH and nitric oxide free radical scavenging activities when compared to that of cottonseed meal and soybean meal extracts. Ferric thiocyanate and thiobarbituric acid tests results showed rapeseed meal with the highest antioxidant activity (P < 0.01) followed by BHT, cotton seed meal and soybean meal. Rapeseed meal extract in xanthine oxidase and tyrosinase inhibitory assays showed the lowest IC(50) values followed by cottonseed and soybean meals. Anti-inflammatory assay using IFN-γ/LPS stimulated RAW 264.7 cells indicated rapeseed meal is a potent source of anti-inflammatory agent. Correlation analysis showed that phenolics and flavonoids were highly correlated to both antioxidant and anti-inflammatory activities. Rapeseed meal was found to be promising as a natural source of bioactive compounds with high antioxidant, anti-inflammatory, xanthine oxidase and tyrosinase inhibitory activities in contrast to cotton and soybean meals.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors
  9. Fulltext Antioxidant, antimicrobial and tyrosinase inhibitory activities of xanthones isolated from Artocarpus obtusus F.M. Jarrett
    Hashim NM, Rahmani M, Ee GC, Sukari MA, Yahayu M, Amin MA, et al.
    Molecules, 2012;17(5):6071-82.
    PMID: 22614861 DOI: 10.3390/molecules17056071
    One of the most promising plants in biological screening test results of thirteen Artocarpus species was Artocarpus obtusus FM Jarrett and detailed phytochemical investigation of powdered dried bark of the plant has led to the isolation and identification of three xanthones; pyranocycloartobiloxanthone A (1), dihydroartoindonesianin C (2) and pyranocycloartobiloxanthone B (3). These compounds were screened for antioxidant, antimicrobial and tyrosinase inhibitory activities. Pyranocycloartobiloxanthone A (1) exhibited a strong free radical scavenger towards DPPH free radicals with IC50 value of 2 µg/mL with prominent discoloration observed in comparison with standard ascorbic acid, α-tocopherol and quercetin, The compound also exhibited antibacterial activity against methicillin resistant Staphylococcus aureus (ATCC3359) and Bacillus subtilis (clinically isolated) with inhibition zone of 20 and 12 mm, respectively. However the other two xanthones were found to be inactive. For the tyrosinase inhibitory activity, again compound (1) displayed strong activity comparable with the standard kojic acid.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  10. Chemical profile and antiacetylcholinesterase, antityrosinase, antioxidant and α-glucosidase inhibitory activity of Cynometra cauliflora L. leaves
    Ado MA, Abas F, Ismail IS, Ghazali HM, Shaari K
    J Sci Food Agric, 2015 Feb;95(3):635-42.
    PMID: 25048579 DOI: 10.1002/jsfa.6832
    The aim of the current study was (i) to evaluate the bioactive potential of the leaf methanolic extract of Cynometra cauliflora L., along with its respective hexane, dichloromethane, ethyl acetate (EtOAc), n-butanol (n-BuOH) and aqueous fractions, in inhibiting the enzymes α-glucosidase, acetylcholinesterase (AChE) and tyrosinase as well as evaluating their antioxidant activities. (ii) In addition, in view of the limited published information regarding the metabolite profile of C. cauliflora, we further characterized the profiles of the EtOAc and n-BuOH fractions using liquid chromatography-diode array detection-electrospray ionization-tandem mass spectrometry.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  11. Biological activity and molecular docking studies of curcumin-related α,β-unsaturated carbonyl-based synthetic compounds as anticancer agents and mushroom tyrosinase inhibitors
    Bukhari SN, Jantan I, Unsal Tan O, Sher M, Naeem-Ul-Hassan M, Qin HL
    J Agric Food Chem, 2014 Jun 18;62(24):5538-47.
    PMID: 24901506 DOI: 10.1021/jf501145b
    Hyperpigmentation in human skin and enzymatic browning in fruits, which are caused by tyrosinase enzyme, are not desirable. Investigations in the discovery of tyrosinase enzyme inhibitors and search for improved cytotoxic agents continue to be an important line in drug discovery and development. In present work, a new series of 30 compounds bearing α,β-unsaturated carbonyl moiety was designed and synthesized following curcumin as model. All compounds were evaluated for their effects on human cancer cell lines and mushroom tyrosinase enzyme. Moreover, the structure-activity relationships of these compounds are also explained. Molecular modeling studies of these new compounds were carried out to explore interactions with tyrosinase enzyme. Synthetic curcumin-like compounds (2a-b) were identified as potent anticancer agents with 81-82% cytotoxicity. Five of these newly synthesized compounds (1a, 8a-b, 10a-b) emerged to be the potent inhibitors of mushroom tyrosinase, providing further insight into designing compounds useful in fields of food, health, and agriculture.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors
  12. Tyrisonase inhibition and melanin reduction of human melanocytes (HEMn-MP) using Anacardium occidentale L extract
    Abdul Gaffar R, Abdul Majid FA, Sarmidi MR
    Med J Malaysia, 2008 Jul;63 Suppl A:100-1.
    PMID: 19025004
    Cashew (Anacardium occindentale L) leaves extract (CLE) has potential as tyrosinase inhibitor that can be used for therapeutic in pigmentation problem. This study investigates the real potential of CLE to inhibit tyrosinase and melanin reduction using human epidermal melanocytes. The extracts were exposed to the human melanocytes for more than 24 hours. The CLE extract exhibited potential as tyrosinase inhibitor, reduced melanin and high in antioxidant activity relative to commercial extract of Emblica sp.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  13. Isolation and identification of radical scavenging and tyrosinase inhibition of polyphenols from Tibouchina semidecandra L
    Sirat HM, Rezali MF, Ujang Z
    J Agric Food Chem, 2010 Oct 13;58(19):10404-9.
    PMID: 20809630 DOI: 10.1021/jf102231h
    Phytochemical and bioactivity studies of the leaves and stem barks of Tibouchina semidecandra L. have been carried out. The ethyl acetate extract of the leaves yielded four flavonoid compounds, identified as quercetin, quercetin 3-O-α-l-(2''-O-acetyl) arabinofuranoside, avicularin, and quercitrin, while the stem barks gave one ellagitannin, identified as 3,3'-O-dimethyl ellagic acid 4-O-α-l-rhamnopyranoside. Evaluation of the antioxidative activity on the crude extracts and pure compounds by electron spin resonance (ESR) and ultraviolet-visible (UV-vis) spectrophotometric assays showed that the pure isolated polyphenols and the EtOAc extract possessed strong antioxidative capabilities. Quercetin was found to be the most active radical scavenger in DPPH-UV and ESR methods with SC(50) values of 0.7 μM ± 1.4 and 0.7 μM ± 0.6 μM, respectively, in the antioxidant assay. A combination of quercetin and quercitrin was tested for synergistic antioxidative capacity;, however, there was no significant improvement observed. Quercetin also exhibited strong antityrosinase activity with a percent inhibition of 95.0% equivalent to the positive control, kojic acid, in the tyrosinase inhibition assay.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  14. Synthesis and biological activity of oxadiazole and triazolothiadiazole derivatives as tyrosinase inhibitors
    Lam KW, Syahida A, Ul-Haq Z, Abdul Rahman MB, Lajis NH
    Bioorg Med Chem Lett, 2010 Jun 15;20(12):3755-9.
    PMID: 20493688 DOI: 10.1016/j.bmcl.2010.04.067
    A series of 16 oxadiazole and triazolothiadiazole derivatives were designed, synthesized and evaluated as mushroom tyrosinase inhibitors. Five derivatives were found to display high inhibition on the tyrosinase activity ranging from 0.87 to 1.49 microM. Compound 5 exhibited highest tyrosinase inhibitory activity with an IC(50) value of 0.87+/-0.16 microM. The in silico protein-ligand docking using AUTODOCK 4.1 was successfully performed on compound 5 with significant binding energy value of -5.58 kcal/mol. The docking results also showed that the tyrosinase inhibition might be due to the metal chelating effect by the presence of thione functionality in compounds 1-5. Further studies revealed that the presence of hydrophobic group such as cycloamine derivatives played a major role in the inhibition. Piperazine moiety in compound 5 appeared to be involved in an extensive hydrophobic contact and a 2.9A hydrogen bonding with residue Glu 182 in the active site.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  15. Antioxidant activities and tyrosinase inhibition effects of Phaleria macrocarpa extracts
    Nadri MH, Salim Y, Basar N, Yahya A, Zulkifli RM
    Afr J Tradit Complement Altern Med, 2014;11(3):107-11.
    PMID: 25371571
    BACKGROUND: The ethyl acetate and chloroform extracts of stems, leaves and fruits of Phaleria macrocarpa were screened for their antioxidant capacity and tyrosinase inhibition properties.

    MATERIAL AND METHOD: The total phenolic content (TPC), 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging and ferric-ion reducing power (FRAP) were used to evaluate their antioxidant capacity. Tyrosinase inhibition effect was measured using mushroom tyrosinase inhibition assay.

    RESULT: Ethyl acetate extract of P. macrocarpa's stem exhibited highest total phenolic content, DPPH free radical scavenging and ferric reducing power. Meanwhile, chloroform extracts of leaves and fruits demonstrated potent anti-tyrosinase activities as compared to a well-known tyrosinase inhibitor, kojic acid.

    CONCLUSION: Since chloroform extracts of leaves and fruits have low antioxidant capacities, the tyrosinase inhibition effect observed are antioxidant independent. This study suggests direct tyrosinase inhibition by chloroform extracts of Phaleria macrocarpa.

    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  16. Fulltext Antioxidant, antityrosinase, anticholinesterase, and nitric oxide inhibition activities of three malaysian macaranga species
    Mazlan NA, Mediani A, Abas F, Ahmad S, Shaari K, Khamis S, et al.
    ScientificWorldJournal, 2013;2013:312741.
    PMID: 24319356 DOI: 10.1155/2013/312741
    The methanol extracts of three Macaranga species (M. denticulata, M. pruinosa, and M. gigantea) were screened to evaluate their total phenolic contents and activities as cholinesterase inhibitors, nitric oxide (NO) production inhibitors, tyrosinase inhibitors, and antioxidants. The bark of M. denticulata showed the highest total phenolic content (2682 mg gallic acid equivalent (GAE)/100 g) and free radical scavenging activity (IC50 = 0.063 mg/mL). All of the samples inhibited linoleic acid peroxidation by greater than 80%, with the leaves of M. gigantea exhibiting the highest inhibition of 92.21%. Most of the samples exhibited significant antioxidant potential. The bark of M. denticulata and the leaves of both M. pruinosa and M. gigantea exhibited greater than 50% tyrosinase inhibition, with the bark of M. denticulata having the highest percentage of inhibition (68.7%). The bark and leaves of M. denticulata exhibited greater than 50% inhibition (73.82% and 54.50%, resp.) of the acetylcholinesterase enzyme (AChE), while none of the samples showed any significant inhibition of butyrylcholinesterase (BChE). Only the bark of M. denticulata and M. gigantea displayed greater than 50% inhibition of nitric oxide production in cells (81.79% and 56.51%, resp.). These bioactivities indicate that some Macaranga spp. have therapeutic potential in medicinal research.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  17. Deciphering the toxicological and computational assessment of Verbascum yemenese.: Integrating phytochemistry and bioinformatics tools
    Alghamdi A, A Awadh Ali N, Alafnan A, Zainal Abidin SA, Alamri A, Hussein W, et al.
    Food Chem Toxicol, 2024 Nov;193:115028.
    PMID: 39368542 DOI: 10.1016/j.fct.2024.115028
    This study explores the phytochemical composition and biological activities of Verbascum yemenense, a plant known for its medicinal properties. The plant extract revealed a rich presence of bioactive compounds that exhibited significant antioxidant properties against free radicals. The enzyme inhibition potential was particularly notable against cholinesterases (AChE: 2.56 mg GALAE/g; BChE: 1.98 mg GALAE/g), and tyrosinase (87.94 mg KAE/g), α-glucosidase suggesting potential therapeutic applications in neurodegenerative diseases, skin disorders and diabetes. Molecular docking studies and Molecular Dynamics simulations, providing insights into the interaction mechanisms of the identified compounds with the target proteins. Molecular docking studies revealed high binding affinities of the phytoconstituents, with compounds like VY4 and phyllanthusol-A (VY15) showing substantial docking scores against AChE (-9.840 kcal/mol) and BChE (-9.853 kcal/mol), respectively. For instance, the RMSD values during the MD simulations for compound VY17 in the AML complex showed a stable conformation, fluctuating within a range of 0.75 Å to 1.75 Å, indicating a strong and consistent interaction with the enzyme. MESP studies highlighted VY17's distinctive electrostatic features, notably a pronounced electronegative region, which might contribute to its binding efficiency. These findings suggest that V. yemenense is a promising candidate for developing novel therapeutic agents.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors
  18. Synthesis and structure-activity relationship of tyrosinase inhibiting novel bi-heterocyclic acetamides: Mechanistic insights through enzyme inhibition, kinetics and computational studies
    Butt ARS, Abbasi MA, Aziz-Ur-Rehman, Siddiqui SZ, Raza H, Hassan M, et al.
    Bioorg Chem, 2019 05;86:459-472.
    PMID: 30772647 DOI: 10.1016/j.bioorg.2019.01.036
    The present research was designed for the selective synthesis of novel bi-heterocyclic acetamides, 9a-n, and their tyrosinase inhibition to overwhelm the problem of melanogenesis. The structures of newly synthesized compounds were confirmed by spectral techniques such as 1H NMR, 13C NMR, and EI-MS along with elemental analysis. The inhibitory effects of these bi-heterocyclic acetamides (9a-n) were evaluated against tyrosinase and all these molecules were recognized as potent inhibitors relative to the standard used. The Kinetics mechanism was analyzed by Lineweaver-Burk plots which explored that compound, 9h, inhibited tyrosinase competitively by forming an enzyme-inhibitor complex. The inhibition constants Ki calculated from Dixon plots for this compound was 0.0027 µM. The computational study was coherent with the experimental records and these ligands exhibited good binding energy values (kcal/mol). The hemolytic analysis revealed their mild cytotoxicity towards red blood cell membranes and hence, these molecules can be pondered as nontoxic medicinal scaffolds for skin pigmentation and related disorders.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
  19. New insights into the phytochemical composition, enzyme inhibition and antioxidant properties of desert cotton (Aerva javanica (Bum.f) Shult. -Amaranthaceae)
    Saleem H, Zengin G, Khan KU, Ahmad I, Waqas M, Mahomoodally FM, et al.
    Nat Prod Res, 2021 Feb;35(4):664-668.
    PMID: 30919661 DOI: 10.1080/14786419.2019.1587427
    This study sets out to probe into total bioactive contents, UHPLC-MS secondary metabolites profiling, antioxidant (DPPH, ABTS, FRAP, CUPRAC, phosphomolybdenum and metal chelating) and enzyme inhibitory (acetylcholinesterase- AChE, butyrylcholinesterase- BChE, α-amylase, α glucosidase, and tyrosinase) activities of methanol extract of Aerva javanica, also known as desert cotton or Kapok bush. Aerva javanica contains considerable phenolic (44.79 ± 3.12 mg GAE/g) and flavonoid (28.86 ± 0.12 mg QE/g) contents which tends to correlate with its significant antioxidant potential for ABTS, FRAP and CUPRAC assays with values of 101.41 ± 1.18, 124.10 ± 1.71 and 190.22 ± 5.70 mg TE/g, respectively. The UHPLC-MS analysis identified the presence of 45 phytochemicals belonging to six major groups: phenolic, flavonoids, lignin, terpenes, glycoside and alkaloid. Moreover, the plant extract also showed potent inhibitory action against AChE (3.73 ± 0.22 mg GALAE/g), BChE (3.31 ± 0.19 mg GALAE/g) and tyrosinase (126.05 ± 1.77 mg KAE/g). The observed results suggest A. javanica could be further explored as a natural source of bioactive compounds.
    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors
  20. Evaluation of Cytotoxic and Tyrosinase Inhibitory Activities of 2-phenoxy(thiomethyl) pyridotriazolopyrimidines: In Vitro and Molecular Docking Studies
    Abuelizz HA, Anouar EH, Marzouk M, Hasan MH, Saleh SR, Ahudhaif A, et al.
    Anticancer Agents Med Chem, 2020;20(14):1714-1721.
    PMID: 32593283 DOI: 10.2174/1871520620666200627212128
    BACKGROUND: The use of tyrosinase has confirmed to be the best means of recognizing safe, effective, and potent tyrosinase inhibitors for whitening skin. Twenty-four 2-phenoxy(thiomethyl)pyridotriazolopyrimidines were synthesized and characterized in our previous studies.

    OBJECTIVE: The present work aimed to evaluate their cytotoxicity against HepG2 (hepatocellular carcinoma), A549 (pulmonary adenocarcinoma), MCF-7 (breast adenocarcinoma) and WRL 68 (embryonic liver) cell lines.

    METHODS: MTT assay was employed to investigate the cytotoxicity, and a tyrosinase inhibitor screening kit was used to evaluate the Tyrosinase (TYR) inhibitory activity of the targets.

    RESULTS: The tested compounds exhibited no considerable cytotoxicity, and nine of them were selected for a tyrosinase inhibitory test. Compounds 2b, 2m, and 5a showed good inhibitory percentages against TYR compared to that of kojic acid (reference substance). Molecular docking was performed to rationalize the Structure-Activity Relationship (SAR) of the target pyridotriazolopyrimidines and analyze the binding between the docked-selected compounds and the amino acid residues in the active site of tyrosinase.

    CONCLUSION: The target pyridotriazolopyrimidines were identified as a new class of tyrosinase inhibitors.

    Matched MeSH terms: Monophenol Monooxygenase/antagonists & inhibitors*
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