Thielavins A, J and K: A-Glucosidase inhibitors from MEXU 27095, an endophytic fungus from Hintonia latiflora

Phytochemistry

Volumn 94, Issue , 2013, Pages 198-205

  Rivera Chávez, José ^a   González Andrade, Martín ^b   Del Carmen González, María ^a   Glenn, Anthony E ^c   Mata, Rachel ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b INSTITUTO NACIONAL DE MEDICINA GENÓMICA   (Mexico)

^c RUSSELL RESEARCH CENTER   (United States)

Author keywords

Endophytic fungus; Enzymatic inhibition; Hintonia latiflora; Molecular docking; Oral sucrose tolerance test; Thielavins; Type II diabetes mellitus; Glucosidase

Indexed keywords

FUNGI; GEOBACILLUS STEAROTHERMOPHILUS; HINTONIA LATIFLORA; MUS; RUBIA; SACCHAROMYCES;

ACARBOSE; ALPHA GLUCOSIDASE; ANTIDIABETIC AGENT; ENZYME INHIBITOR; HYDROXYBENZOIC ACID DERIVATIVE; THIELAVIN A; THIELAVIN J; THIELAVIN K;

ANIMAL; ARTICLE; ASCOMYCETES; BLOOD; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG ANTAGONISM; ENDOPHYTIC FUNGUS; ENZYMATIC INHIBITION; ENZYMOLOGY; EXPERIMENTAL DIABETES MELLITUS; GLUCOSE BLOOD LEVEL; HINTONIA LATIFLORA; INSTITUTE FOR CANCER RESEARCH MOUSE; ISOLATION AND PURIFICATION; KINETICS; MALE; MEDICINAL PLANT; METABOLISM; MEXICO; MICROBIOLOGY; MOLECULAR DOCKING; NON INSULIN DEPENDENT DIABETES MELLITUS; ORAL SUCROSE TOLERANCE TEST; PHYTOTHERAPY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; RUBIACEAE; SACCHAROMYCES CEREVISIAE; THIELAVINS; TREATMENT OUTCOME; TYPE II DIABETES MELLITUS; Α-GLUCOSIDASE;

ENDOPHYTIC FUNGUS; ENZYMATIC INHIBITION; HINTONIA LATIFLORA; MOLECULAR DOCKING; ORAL SUCROSE TOLERANCE TEST; THIELAVINS; TYPE II DIABETES MELLITUS; Α-GLUCOSIDASE;

ACARBOSE; ALPHA-GLUCOSIDASES; ANIMALS; ASCOMYCOTA; BLOOD GLUCOSE; DIABETES MELLITUS, EXPERIMENTAL; DIABETES MELLITUS, TYPE 2; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; HYDROXYBENZOATES; HYPOGLYCEMIC AGENTS; KINETICS; MALE; MEXICO; MICE, INBRED ICR; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PHYTOTHERAPY; PLANTS, MEDICINAL; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RUBIACEAE; SACCHAROMYCES CEREVISIAE; TREATMENT OUTCOME;

EID: 84885181923     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2013.05.021     Document Type: Article

References (29)

1. Benalla, W., Bellahcen, S., Bnouham, M., 2010. Antidiabetic medicinal plants as a source of alpha glucosidase inhibitors. Curr. Diabetes Rev. 6, 247-254.
2. Chen, L., Magliano, D.J., Zimmet, P.Z., 2011. The worldwide epidemiology of type 2 diabetes mellitus-present and future perspectives. Nature Publishing Group 8, 228-236.
3. Copeland, R.A., 2000. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis, second ed. Wiley-VCH.
4. Çifci, G., Aviyente, V., Akten, E.D., 2012. Molecular Docking study based on pharmacophore modeling for novel phosphodiesterase IV inhibitors. Mol. Inf. 31, 459-471.
5. De Lano, W., Scientific, L.D., 2002. De Lano: PyMOL version 0.99, DeLano Scientific.
6. Escandón-Rivera, S., González-Andrade, M., Bye, R., Linares, E., Navarrete, A., Mata, R., 2012. α-Glucosidase inhibitors from Brickellia cavanillesii. J. Nat. Prod. 75, 968-974.
7. Guerrero-Analco, J., Medina-Campos, O., Brindis, F., Bye, R., Pedraza-Chaverri, J., Navarrete, A., Mata, R., 2007. Antidiabetic properties of selected Mexican copalchis of the Rubiaceae family. Phytochemistry 68, 2087-2095.
8. Israili, Z.H., 2011. Advances in the treatment of type 2 diabetes mellitus. Am. J. Ther. 18, 117-152.
9. Kitahara, N.N., Endo, A.A., Furuya, K.K., Takahashi, S.S., 1981. Thielavin A and B, new inhibitors of prostaglandin biosynthesis produced by Thielavia terricola. J. Antibiot. 34, 1562-1568.
10. Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
11. Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R., Thornton, J.M., 1996. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
12. Mata, R., Cristians, S., Escandón-Rivera, S., Juárez-Reyes, K., Rivero-Cruz, I., 2013. Mexican antidiabetic herbs: valuable sources of inhibitors of α-glucosidases. J. Nat. Prod. 130304132955004.
13. Miller, K.I., Qing, C., Sze, D.M.-Y., Roufogalis, B.D., Neilan, B.A., 2012. Culturable endophytes of medicinal plants and the genetic basis for their bioactivity. Microb. Ecol. 64, 431-449.
14. Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., Olson, A.J., 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19, 1639-1662.
15. Nakai, H., Okuyama, M., Kim, Y., Saburi, W., Wongchawalit, J., Mori, H., Chiba, S., Kimura, A., 2005. Molecular analysis of a-glucosidase belonging to GH-family 31. Biologia, Bratislava 60, 131-135.
16. Oki, T., Matsui, T., Osajima, Y., 1999. Inhibitory effect of α-glucosidase, inhibitors varies according to its origin. J. Agric. Food Chem. 47, 550-553.
17. Rodriguez, R.J., White Jr, J.F., Arnold, A.E., Redman, R.S., 2009. Fungal endophytes: diversity and functional roles. New Phytol. 182, 314-330.
18. Rudnitskaya, A., Török, B., Török, M., 2010. Molecular docking of enzyme inhibitors. Biochem. Mol. Biol. Educ. 38, 261-265.
19. Sakemi, S.S., Hirai, H.H., Ichiba, T.T., Inagaki, T.T., Kato, Y.Y., Kojima, N.N., Nishida, H.H., Parker, J.C.J., Saito, T.T., Tonai-Kachi, H.H., VanVolkenburg, M.A.M., Yoshikawa, N.N., Kojima, Y.Y., 2002. Thielavins as glucose-6-phosphatase (G6Pase) inhibitors: producing strain, fermentation, isolation, structural elucidation and biological activities. J. Antibiot. 55, 941-951.
20. Scully, T., 2012. Diabetes in numbers. Nature 485, S2-S3.
21. Segel, I.H., 1993. Enzyme Kinetics. Wiley-Interscience.
22. Shirai, T., Hung, V.S., Morinaka, K., Kobayashi, T., Ito, S., 2008. Crystal structure of GH13 α-glucosidase GSJ from one of the deepest sea bacteria. Proteins 73, 126-133.
23. Sim, L., Jayakanthan, K., Mohan, S., Nasi, R., Johnston, B.D., Pinto, B.M., Rose, D.R., 2010. New glucosidase inhibitors from an Ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from salacia reticulata. Biochemistry 49, 443-451.
24. Suzuki, Y., Shinji, M., Eto, N., 1984. Assignment of a p-nitrophenyl α-D-glucopyranosidase of Bacillus stearothermophilus ATCC 12016 to a novel exo-α-1, 4-glucosidase active for oligomaltosaccharides and α-glucans. Biochim. Biophys. Acta (BBA) - Protein Struct. Mol. Enzymol. 787, 281-289.
25. Takii, Y., Takahashi, K., Yamamoto, K., Sogabe, Y., Suzuki, Y., 1996. Bacillus stearothermophilus ATCC12016 α-glucosidase specific for α-1,4 bonds of maltosaccharides and α-glucans shows high amino acid sequence similarities to seven α-D-glucohydrolases with different substrate specificity. Appl. Microbiol. Biotechnol. 44, 629-634.
26. Tsujimoto, Y., Tanaka, H., Takemura, R., Yokogawa, T., Shimonaka, A., Matsui, H., Kashiwabara, S.I., Watanabe, K., Suzuki, Y., 2007. Molecular determinants of substrate recognition in thermostable α-glucosidases belonging to glycoside hydrolase family 13. J. Biochem. 142, 87-93.
27. Verspohl, E.J., 2002. Recommended testing in diabetes research. Planta Med. 68, 581-590.
28. Wardrop, D.J., Waidyarachchi, S.L., 2010. Synthesis and biological activity of naturally occurring α-glucosidase inhibitors. Nat. Prod. Rep. 27, 1431.
29. Xu, H., 2010. Inhibition kinetics of flavonoids on yeast-glucosidase merged with docking simulations. Protein Pept. Lett. 17, 1270-1279.