Structure-activity relationships of bergenin derivatives effect on α-glucosidase inhibition

References

• Porte D Jr. Banting lecture 1990. β-cells in type II diabetes mellitus. Diabetes 1991;40:166–180.
   PubMed Web of Science ®Google Scholar
• Taylor SI, Accili D, Imai Y. Insulin resistance or insulin deficiency. Which is the primary cause of NIDDM? Diabetes 1994;43:735–740.
   PubMed Web of Science ®Google Scholar
• O’Dea K, Turton J. Optimum effectiveness of intestinal α-glucosidase inhibitors: importance of uniform distribution through a meal. Am J Clin Nutr 1985;41:511–516.
   PubMedGoogle Scholar
• Samad AH, Ty Willing TS, Alberti KG, Taylor R. Effects of BAYm 1099, new α-glucosidase inhibitor, on acute metabolic responses and metabolic control in NIDDM over 1 mo. Diabetes Care 1988;11:337–344.
   PubMedGoogle Scholar
• Bischoff H. The mechanism of α-glucosidase inhibition in the management of diabetes. Clin Invest Med 1995;18:303–311.
   PubMed Web of Science ®Google Scholar
• Floris AL, Peter LL, Reinier PA, Eloy HL, Guy ER, Chris W. α-glucosidase inhibitors for patients with type 2 diabetes: results from a Cochrane systematic review and meta-analysis. Diabetes Care 2005;28:154–163.
   PubMedGoogle Scholar
• Fernandes B, Sagman U, Auger M, Demetrio M, Dennis JW. β 1-6 branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia. Cancer Res 1991;51:718–723.
   PubMed Web of Science ®Google Scholar
• Ozawa S, Maruyama A, Odagiri T, Yuasa H, Hashimoto H. Synthesis and biological evaluation of α-l-fucosidase inhibitors: 5a-carba-a-l-fucopyranosylamine and related compounds. Eur J Org Chem 2001;5:967–974.
   Google Scholar
• Humphries MJ, Matsumoto K, White SL, Olden K. Inhibition of experimental metastasis by castanospermine in mice: blockage of two distinct stages of tumor colonization by oligosaccharide processing inhibitors. Cancer Res 1986;46:5215–5222.
   PubMed Web of Science ®Google Scholar
• Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG et al. Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. Nature 1987;330:74–77.
   PubMed Web of Science ®Google Scholar
• Tattersall R. α-glucosidase inhibition as an adjunct to the treatment of type 1 diabetes. Diabet Med 1993;10:688–693.
   PubMedGoogle Scholar
• Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR. Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. J Mol Biol 2008;375:782–792.
   PubMed Web of Science ®Google Scholar
• Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1991;280 (Pt 2):309–316.
   PubMedGoogle Scholar
• Henrissat B, Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem J 1996;316 (Pt 2):695–696.
   PubMedGoogle Scholar
• Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 1995;92:7090–7094.
   PubMed Web of Science ®Google Scholar
• Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng Des Sel 2006;19:555–562.
   PubMed Web of Science ®Google Scholar
• Henrissat B, Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 1997;7:637–644.
   PubMed Web of Science ®Google Scholar
• Ly HD, Withers SG. Mutagenesis of glycosidases. Annu Rev Biochem 1999;68:487–522.
   PubMed Web of Science ®Google Scholar
• Park H, Hwang KY, Oh KH, Kim YH, Lee JY, Kim K. Discovery of novel α-glucosidase inhibitors based on the virtual screening with the homology-modeled protein structure. Bioorg Med Chem 2008;16:284–292.
   PubMed Web of Science ®Google Scholar
• Pluempanupat W, Adisakwattana S, Yibchok-Anun S, Chavasiri W. Synthesis of N-phenylphthalimide derivatives as α-glucosidase inhibitors. Arch Pharm Res 2007;30:1501–1506.
   PubMed Web of Science ®Google Scholar
• Zhang R, McCarter JD, Braun C, Yeung W, Brayer GD, Withers SG. Synthesis and testing of 2-deoxy-2,2-dihaloglycosides as mechanism-based inhibitors of α-glycosidases. J Org Chem 2008;73:3070–3077.
   PubMedGoogle Scholar
• Choi CW, Choi YH, Cha MR, Yoo DS, Kim YS, Yon GH et al. Yeast α-glucosidase inhibition by isoflavones from plants of Leguminosae as an in vitro alternative to acarbose. J Agric Food Chem 2010;58:9988–9993.
   PubMed Web of Science ®Google Scholar
• Kim JY, Lee JW, Kim YS, Lee Y, Ryu YB, Kim S et al. A novel competitive class of α-glucosidase inhibitors: (E)-1-phenyl-3-(4-styrylphenyl)urea derivatives. Chembiochem 2010;11:2125–2131.
   PubMed Web of Science ®Google Scholar
• Li GL, He JY, Zhang A, Wan Y, Wang B, Chen WH. Toward potent α-glucosidase inhibitors based on xanthones: a closer look into the structure-activity correlations. Eur J Med Chem 2011;46:4050–4055.
   PubMed Web of Science ®Google Scholar
• Bahl CP, Murari R, Parthasarathy MR, Seshadri TR. Components of Bergenia strecheyi and B. ligulata. Ind J Chem 1974;12:1038–1039.
   Google Scholar
• Tucci AP, Delle Monache F, Marini-Bettòlo GB. The occurrence of (+)afzelechin in Saxifraga ligulata Wall. Ann Ist Super Sanita 1969;5:555–556.
   PubMedGoogle Scholar
• Dixit BS, Srivastava SN. Tannin constituents of Bergenia ligulata roots. Ind J Nat Prod 1989;5:24–25.
   Google Scholar
• Chandrareddy UD, Chawla AS, Mundkinajeddu D, Maurya R, Handa SS. Paashaanolactone from Bergenia ligulata. Phytochemistry 1998;47:907–909.
   Google Scholar
• Kashima Y, Yamaki H, Suzuki T, Miyazawa M. Insecticidal effect and chemical composition of the volatile oil from Bergenia ligulata. J Agric Food Chem 2011;59:7114–7119.
   PubMedGoogle Scholar
• Swarnalakshmi T, Sethuraman MG, Sulochana N, Arivudainambi R. A note on the anti-inflammatory activity of bergenin. Curr Sci 1984;53:917.
   Web of Science ®Google Scholar
• Afran M, Amin H, Karamac M, Kosinska A, Wiczkowski W, Amarowicz R. Antioxidant activity of phenolic fractions of Mallotus philippinensis bark extract. Czech J Food Sci 2009;27:109–117.
   Google Scholar
• Jahromi MAF, Chansouri JPN, Ray AB. Hypolipidaemic activity in rats of bergenin, the major constituent of Flueggea microcarpa. Phytother Res 1992;6:180–183.
   Web of Science ®Google Scholar
• Takahashi H, Kosaka M, Watanabe Y, Nakade K, Fukuyama Y. Synthesis and neuroprotective activity of bergenin derivatives with antioxidant activity. Bioorg Med Chem 2003;11:1781–1788.
   PubMed Web of Science ®Google Scholar
• Piacente S, Pizza C, De Tommasi N, Mahmood N. Constituents of Ardisia japonica and their in vitro anti-HIV activity. J Nat Prod 1996;59:565–569.
   PubMed Web of Science ®Google Scholar
• Pu HL, Huang X, Zhao JH, Hong A. Bergenin is the antiarrhythmic principle of Fluggea virosa. Planta Med 2002;68:372–374.
   PubMed Web of Science ®Google Scholar
• Prithiviraj B, Singh UP, Manickam M, Srivastava JS, Ray AB. Antifungal activity of bergenin, a constituent of Flueggea microcarpa. Plant Pathol 1997;46:224–228.
   Google Scholar
• Goel RK, Maiti RN, Manickam M, Ray AB. Antiulcer activity of naturally occurring pyrano-coumarin and isocoumarins and their effect on prostanoid synthesis using human colonic mucosa. Indian J Exp Biol 1997;35:1080–1083.
   PubMedGoogle Scholar
• Lee YY, Jang DS, Jin JL, Yun-Choi HS. Anti-platelet aggregating and anti-oxidative activities of 11-O-(4′-O-methylgalloyl)-bergenin, a new compound isolated from Crassula cv. ‘Himaturi’. Planta Med 2005;71:776–777.
   PubMed Web of Science ®Google Scholar
• Jia Z, Mitsunaga K, Koike K, Ohmoto T. New bergenin derivatives from Ardisia crenata. Nat Med 1995;49:187–189.
   Google Scholar
• Fuji M, Miyaichi Y, Tomimori T. Studies on nepalese crude drugs. XXII on the phnolic constituents of the rhizome of Bergenia ciliata (Haw.) STERNB. Nat Med 1996;50:404–407.
   Google Scholar
• Saijo R, Nonaka G, Nishioka I. Gallic acid esters of bergenin and norbergenin from Mallotus japonicus. Phytochemistry 1990;29:267–270.
   Web of Science ®Google Scholar
• Yoshida T, Seno K, Takama Y, Okuda T. Bergenin derivatives from Mallotus japonicus. Phytochemistry 1982;21:1180–1182.
   Web of Science ®Google Scholar
• Girard N, Rousseau C, Martin OR. Intramolecular C-glycosylation of 2-O-benzylated pentenyl mannopyranosides: remarkable 1, 2-trans stereoselectivity. Tetrahedron Lett 2003;44:8971–8974.
   Google Scholar
• Wang D, Zhu HT, Zhang YJ, Yang CR. A carbon-carbon-coupled dimeric bergenin derivative biotransformed by Pleurotus ostreatus. Bioorg Med Chem Lett 2005;15:4073–4075.
   PubMed Web of Science ®Google Scholar
• Pearl IA. Vanilic acid. Org Synth 1963;4:972–977.
   Google Scholar
• Li W, Wei K, Fu H, Koike K. Structure and absolute configuration of clerodane diterpene glycosides and a rearranged cadinane sesquiterpene glycoside from the stems of Tinospora sinensis. J Nat Prod 2007;70:1971–1976.
   PubMedGoogle Scholar
• Liang PH, Cheng WC, Lee YL, Yu HP, Wu YT, Lin YL et al. Novel five-membered iminocyclitol derivatives as selective and potent glycosidase inhibitors: new structures for antivirals and osteoarthritis. Chembiochem 2006;7:165–173.
   PubMed Web of Science ®Google Scholar
• Adisakwattana S, Sookkongwaree K, Roengsumran S, Petsom A, Ngamrojnavanich N, Chavasiri W et al. Structure-activity relationships of trans-cinnamic acid derivatives on α-glucosidase inhibition. Bioorg Med Chem Lett 2004;14:2893–2896.
   PubMed Web of Science ®Google Scholar
• Oki T, Matsui T, Osajima Y. Inhibitory effect of α-glucosidase inhibitors varies according to its origin. J Agric Food Chem 1999;47:550–553.
   PubMed Web of Science ®Google Scholar