Login Register Cart 0
Generic placeholder image

Current Diabetes Reviews

Editor-in-Chief

ISSN (Print): 1573-3998
ISSN (Online): 1875-6417

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Review Article

An Insight of Alpha-amylase Inhibitors as a Valuable Tool in the Management of Type 2 Diabetes Mellitus

Author(s): Roqia Bashary, Manish Vyas, Surendra Kumar Nayak, Ashish Suttee, Surajpal Verma, Rakesh Narang and Gopal L. Khatik*

Volume 16, Issue 2, 2020

Page: [117 - 136] Pages: 20

DOI: 10.2174/1573399815666190618093315

Price: $65

Abstract

Background: Among the millions of people around the world, the most prevalent metabolic disorder is diabetes mellitus. Due to the drawbacks which are associated with commercially available antidiabetic agents, new therapeutic approaches are needed to be considered. Alpha-amylase is a membrane- bound enzyme which is responsible for the breakdown of polysaccharides such as starch to monosaccharides which can be absorbed.

Methods: We searched the scientific database using alpha-amylase, diabetes, antidiabetic agents as the keywords. Here in, only peer-reviewed research articles were collected which were useful to our current work.

Results: To overcome the research gap, the alpha-amylase enzyme is regarded as a good target for antidiabetic agents to design the drug and provide an alternate approach for the treatment of type 2 diabetes mellitus. Basically, alpha-amylase inhibitors are classified into two groups: proteinaceous inhibitors, and non-proteinaceous inhibitors. Recently, non-proteinaceous inhibitors are being explored which includes chalcones, flavones, benzothiazoles, etc. as the potential antidiabetic agents.

Conclusion: Herein, we discuss various potential antidiabetic agents which are strategically targeted alpha-amylase enzyme. These are having lesser side effects as compared to other antidiabetic agents, and are proposed to prevent the digestion and absorption of glucose leading to a decrease in the blood glucose level.

Keywords: Diabetes, alpha-amylase, alpha-amylase inhibitor, antidiabetic agents, hyperglycemia, hypoglycemia.

[1]
Adeghate E. Medicinal chemistry of novel anti-diabetic drugs. Open Med Chem J 2011; 5(Suppl. 2): 68-9.
[http://dx.doi.org/10.2174/1874104501105010068] [PMID: 21966326]
[2]
Khatik GL, Datusalia AK, Ahsan W, et al. A retrospect study on thiazole derivatives as the potential antidiabetic agents in drug discovery & developments. Curr Drug Discov Technol 2018; 15(3): 163-77.
[http://dx.doi.org/10.2174/1570163814666170915134018] [PMID: 28914188]
[3]
Ozougwo JC, Obimba KC, Belonwu CD, Unakalamba CB. The pathogenesis of type 1 and type 2 diabetes mellitus. J Physiol Pathophysiol 2013; 4(4): 46-57.
[http://dx.doi.org/10.5897/JPAP2013.0001]
[4]
Alagesan K, Raghupathi PK, Sankarnarayanan S. Amylase inhibitors: Potential source of anti-diabetic drug discovery from medicinal plants. Int J Pharm Life Sci 2012; 3(2): 1407-12.
[5]
Baynest HW. Classification, pathophysiology, diagnosis and management of diabetes mellitus. J Diabetes Metab 2015; 6(5): 1-9.
[http://dx.doi.org/10.4172/2155-6156.1000541]
[6]
Nattrass M, Bailey CJ. New agents for Type 2 diabetes. Best Pract Res Clin Endocrinol Metab 1999; 13(2): 309-29.
[http://dx.doi.org/10.1053/beem.1999.0023] [PMID: 10761869]
[7]
Mane PB, Antre RV, Oswal RJ. Antidiabetic drugs: An overview. Int J Pharm Chem Sci 2012; 1(1): 301-6.
[8]
Rendell M. The role of sulphonylureas in the management of type 2 diabetes mellitus. Drugs 2004; 64(12): 1339-58.
[http://dx.doi.org/10.2165/00003495-200464120-00006] [PMID: 15200348]
[9]
Bösenberg LH, Zyl DGV. The mechanism of action of oral antidiabetic drugs: A review on recent literature. J Endocrinol Metab Diab South Africa 2014; 13(3): 80-8.
[http://dx.doi.org/10.1080/22201009.2008.10872177]
[10]
Sundaram A, Anand Moses CR, Ilango S, Seshiah V. Newer antidiabetic drugs. Int J Diab Dev 1998; 18: 24-30.
[11]
Khatik GL. Diabetes mellitus: Recent advancement in ppar agonists as therapeutic agents. Int J Pharma Bio Sci 2015; 6(4): 46-69.
[12]
Das S, Singh S, Sharma V, Soni ML. Biological application of industrially important amylase enzyme. Int J Pharma Bio Sci 2011; 2(1): 486-96.
[13]
Agarwal P, Gupta R. Alpha-amylase inhibition can treat diabetes mellitus. Res Rev J Med Health Sci 2016; 5(4): 1-8.
[14]
de Souza PM, de Oliveira Magalhães P. Application of microbial α-amylase in industry - A review. Braz J Microbiol 2010; 41(4): 850-61.
[http://dx.doi.org/10.1590/S1517-83822010000400004] [PMID: 24031565]
[15]
Kandra L. Alpha-amylases of medical and industrial importance. J Mol Struct THEOCHEM 2003; 666-7: 487-98.
[http://dx.doi.org/10.1016/j.theochem.2003.08.073]
[16]
Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial alpha-amylases: A biotechnological perspective. Process Biochem 2003; 38(11): 1599-616.
[http://dx.doi.org/10.1016/S0032-9592(03)00053-0]
[17]
Whitcomb DC, Lowe ME. Human pancreatic digestive enzymes. Dig Dis Sci 2007; 52(1): 1-17.
[http://dx.doi.org/10.1007/s10620-006-9589-z] [PMID: 17205399]
[18]
Nielsen MM, Bozonnet S, Seo ES, et al. Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules. Biochemistry 2009; 48(32): 7686-97.
[http://dx.doi.org/10.1021/bi900795a] [PMID: 19606835]
[19]
Kirchmair J, Wolber G, Laggner C, Langer T. Comparative performance assessment of the conformational model generators omega and catalyst: A large-scale survey on the retrieval of protein-bound ligand conformations. J Chem Inf Model 2006; 46(4): 1848-61.
[http://dx.doi.org/10.1021/ci060084g] [PMID: 16859316]
[20]
Westerfors M, Tedebark U, Andersson HO, et al. Structure-based discovery of a new affinity ligand to pancreatic alpha-amylase. J Mol Recognit 2003; 16(6): 396-405.
[http://dx.doi.org/10.1002/jmr.626] [PMID: 14732931]
[21]
Patil VS, Nandre KP, Ghosh S, et al. Synthesis, crystal structure and antidiabetic activity of substituted (E)-3-(Benzo [d]thiazol-2-ylamino) phenylprop-2-en-1-one. Eur J Med Chem 2013; 59: 304-9.
[http://dx.doi.org/10.1016/j.ejmech.2012.11.020] [PMID: 23262035]
[22]
Pujadas G, Palau J. Evolution of alpha-amylases: Architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold. Mol Biol Evol 2001; 18(1): 38-54.
[http://dx.doi.org/10.1093/oxfordjournals.molbev.a003718] [PMID: 11141191]
[23]
Wisessing A, Choowongkomon K. Amylase inhibitors in plants: structures, functions and applications. Funct Plant Sci Biotechnol 2011; 6: 31-41.
[24]
Geng P, Qiu F, Zhu Y, Bai G. Four acarviosin-containing oligosaccharides identified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of alpha-amylase. Carbohydr Res 2008; 343(5): 882-92.
[http://dx.doi.org/10.1016/j.carres.2008.01.020] [PMID: 18294624]
[25]
Geng P, Bai G, Shi Q, Zhang L, Gao Z, Zhang Q. Taxonomy of the Streptomyces strain ZG0656 that produces acarviostatin alpha-amylase inhibitors and analysis of their effects on blood glucose levels in mammalian systems. J Appl Microbiol 2009; 106(2): 525-33.
[http://dx.doi.org/10.1111/j.1365-2672.2008.04021.x] [PMID: 19054225]
[26]
Geng P, Bai G. Two novel aminooligosaccharides isolated from the culture of Streptomyces coelicoflavus ZG0656 as potent inhibitors of alpha-amylase. Carbohydr Res 2008; 343(3): 470-6.
[http://dx.doi.org/10.1016/j.carres.2007.11.012] [PMID: 18054350]
[27]
Geng P, Sun T, Zhong Q, et al. Two novel potent α-amylase inhibitors from the family of acarviostatins isolated from the culture of Streptomyces coelicoflavus ZG0656. Chem Biodivers 2013; 10(3): 452-9.
[http://dx.doi.org/10.1002/cbdv.201100451] [PMID: 23495161]
[28]
Vermerris W, Nicholson R. Capter 1: Families of phenolic compounds and means of classification, in phenolic Compound Biochemistry. In: Vermerris W, Nicholson R, Eds. Springer. Dordrecht 2008; pp. 1-34.
[29]
Ghosh D, Scheepens A. Vascular action of polyphenols. Mol Nutr Food Res 2009; 53(3): 322-31.
[http://dx.doi.org/10.1002/mnfr.200800182] [PMID: 19051188]
[30]
Xiao J, Ni X, Kai G, Chen X. A review on structure-activity relationship of dietary polyphenols inhibiting α-amylase. Crit Rev Food Sci Nutr 2013; 53(5): 497-506.
[http://dx.doi.org/10.1080/10408398.2010.548108] [PMID: 23391016]
[31]
Lo Piparo E, Scheib H, Frei N, Williamson G, Grigorov M, Chou CJ. Flavonoids for controlling starch digestion: structural requirements for inhibiting human alpha-amylase. J Med Chem 2008; 51(12): 3555-61.
[http://dx.doi.org/10.1021/jm800115x] [PMID: 18507367]
[32]
Kumari A, Singh K, Kayastha AM. Alpha-amylase: general properties, mechanism and biotechnological applications – A review. Curr Biotechnol 2012; 1(1): 98-107.
[http://dx.doi.org/10.2174/2211550111201010098]
[33]
Takamine J. Enzymes of Aspergillus oryzae and the application of its amyloclastic enzyme to the fermentation industry. Ind Eng Chem Biodivers 1914; 6(10): 824-8.
[http://dx.doi.org/10.1021/ie50070a015]
[34]
Kuriki T, Imanaka T. The concept of the alpha-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng 1999; 87(5): 557-65.
[http://dx.doi.org/10.1016/S1389-1723(99)80114-5] [PMID: 16232518]
[35]
Roberts SC. Production and engineering of terpenoids in plant cell culture. Nat Chem Biol 2007; 3(7): 387-95.
[http://dx.doi.org/10.1038/nchembio.2007.8] [PMID: 17576426]
[36]
Gershenzon J, Dudareva N. The function of terpene natural products in the natural world. Nat Chem Biol 2007; 3(7): 408-14.
[http://dx.doi.org/10.1038/nchembio.2007.5] [PMID: 17576428]
[37]
Ali H, Houghton PJ, Soumyanath A. Alpha-Amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amarus. J Ethnopharmacol 2006; 107(3): 449-55.
[http://dx.doi.org/10.1016/j.jep.2006.04.004] [PMID: 16678367]
[38]
Kim JS, Kwon CS, Son KH. Inhibition of alpha-glucosidase and amylase by luteolin, a flavonoid. Biosci Biotechnol Biochem 2000; 64(11): 2458-61.
[http://dx.doi.org/10.1271/bbb.64.2458] [PMID: 11193416]
[39]
Meyer BH, Müller FO, Clur BK, Grigoleit HG. Effects of tendamistate (alpha-amylase inactivator) on starch metabolism. Br J Clin Pharmacol 1983; 16(2): 145-8.
[http://dx.doi.org/10.1111/j.1365-2125.1983.tb04978.x] [PMID: 6604534]
[40]
Sethi BK. Synthesis and analysis of alpha-amylase inhibitor and antimicrobial Peptide Senior Honors Theses 32
[41]
Dhobale S, Thite T, Laware SL, et al. Zinc oxide nanoparticles as nowel alpha-amylase inhibitors. J Appl Phys 2008; 104(9): 1-5.
[http://dx.doi.org/10.1063/1.3009317]
[42]
Kato E, Chikahisa F, Kawabata J. Synthesis and study of pancreatic alpha-amylase inhibitory activity of methyl acarviosin and its derivatives. Tetrahedron Lett 2016; 57: 1365-7.
[http://dx.doi.org/10.1016/j.tetlet.2016.02.053]
[43]
Rahman MA. Chalcone: A voluable insight into the recent advances and potential pharmacological activities. Chem Sci (Camb) 2011; 2011: 1-16.
[44]
Marulasiddaiah R, Kalkhambkar RG, Kulkarni MV. Synthesis and biological evaluation of cyclic imides with coumarins and azacoumarins. Open J Med Chem 2012; 2: 89-97.
[http://dx.doi.org/10.4236/ojmc.2012.23011]
[45]
Bashary R, Khatik GL. Design, and facile synthesis of 1,3 diaryl-3-(arylamino)propan-1-one derivatives as the potential alpha-amylase inhibitors and antioxidants. Bioorg Chem 2019; 82: 156-62.
[http://dx.doi.org/10.1016/j.bioorg.2018.10.010] [PMID: 30321778]
[46]
Honda T, Kaneno-Urasaki Y, Ito T, et al. Alpha-amylase inhibitor, CS-1036 binds to serum amylase in a concentration-dependent and saturable manner. Drug Metab Dispos 2014; 42(3): 326-33.
[http://dx.doi.org/10.1124/dmd.113.054452] [PMID: 24319124]
[47]
Datar PA, Deokule TA. Design and synthesis of thiadiazole derivatives as antidiabetic agents. Med Chem 2014; 4(4): 390-9.
[48]
Najafian M. The effects of curcumin on alpha-amyalse in diabetes Rats. Zahedan J Res Med Sci 2015; 15: 29-34.
[49]
Bharathi A, Roopan SM, Vasavi CS, Munusami P, Gayathri GA, Gayathri M. In Silico molecular docking and in vitro anti daibetic studies of dihydropyrimido[4,5-a]acridin-2-amines. In: BioMed Res Int 1-9. 2014.
[50]
Shahidpour S, Panahi F, Yousefi R, Nourisefat M, Nabipour M, Khalafi Nezhad A. Design and synthesis of new antidiabetic alpha-glucosidase and alpha-amylase Inhibitors based on pyrimidine-fused heterocycles. Med Chem Res 2015; 24: 3086-96.
[http://dx.doi.org/10.1007/s00044-015-1356-2]
[51]
Ponnusamy S, Haldar S, Mulani F, Zinjarde S, Thulasiram H. RaviKumar A. Gedunin and azadiradione: Human pancreatic alpha-amylase inhibiting limonoids from Neem (Azadirachta indica) as anti-diabetic agents. PLoS One 2015; 10(10)e0140113
[http://dx.doi.org/10.1371/journal.pone.0140113] [PMID: 26469405]
[52]
Asif M. A review on recent advances and potential pharmacological activities of versatile chalcone molecule. Chem Int 2016; 2(1): 1-18.
[53]
Ibrahim SRM, Mohamed GA, Zayed MF, Ross SA. 8-Hydroxyirilone 5-methyl ether and 8-hydroxyirilone, new antioxidant and α-amylase inhibitors isoflavonoids from Iris germanica rhizomes. Bioorg Chem 2017; 70: 192-8.
[http://dx.doi.org/10.1016/j.bioorg.2016.12.010] [PMID: 28069265]
[54]
Nair SMJ, Beevi J. NJM, Emmanuel BD, Dharan SS, CR R. Insilico design, Synthesis and in vitro antidiabetic and anti-inflammatory activities of 1,3,4-Thiadiazole substituted 2-Methyl benzimidazole derivatives. J Pharm Res Clin Pract 2016; 6(1): 27-36.
[55]
Tysoe C, Williams LK, Keyzers R, et al. Potent human alpha-amylase inhibition by the β-Defensin-like protein helianthamide. ACS Cent Sci 2016; 2(3): 154-61.
[http://dx.doi.org/10.1021/acscentsci.5b00399] [PMID: 27066537]
[56]
Noreen T, Taha M, Imran S, et al. Synthesis of alpha amylase inhibitors based on privileged indole scaffold. Bioorg Chem 2017; 72: 248-55.
[http://dx.doi.org/10.1016/j.bioorg.2017.04.010] [PMID: 28482265]
[57]
Subhedar DD, Shaikh MH, Arkile MA, Yeware A, Sarkar D, Shingate BB. Facile synthesis of 1,3-thiazolidin-4-ones as antitubercular agents. Bioorg Med Chem Lett 2016; 26(7): 1704-8.
[http://dx.doi.org/10.1016/j.bmcl.2016.02.056] [PMID: 26927426]
[58]
Pansare DN, Shinde DB. Synthesis and antimicrobial activity of new (Z)-2-((5-(4-hydroxybenzylidene)-4-oxo-4,5-dihydrothiazol-2-yl) amino) acid and its Derivatives. J Med Pharm Innov 2015; 2(8): 23-9.
[59]
Husain A, Rashid M, Shaharyar M, Siddiqui AA, Mishra R. Benzimidazole clubbed with triazolo-thiadiazoles and triazolo-thiadiazines: New anticancer agents. Eur J Med Chem 2013; 62: 785-98.
[http://dx.doi.org/10.1016/j.ejmech.2012.07.011] [PMID: 23333063]
[60]
Siddiqui N, Arya SK, Ahsan W, Azad B. Diverse biological activities of Thiazoles: A Retrospect. Int J Drug Dev Res 2011; 3(4): 55-67.
[61]
Mohammadi A, Ghafoori H, Rassa M, Safarnejad M. Aryl azo 5- arylidene-2,4-thiazolidinone dyes as novel antioxidant and antibacterial compounds. In: Prog Color Colorants Coat. 2015; pp. 145-52.
[62]
Mohammed Iqbal AK, Khan AY, Kalashetti MB, Belavagi NS, Gong YD, Khazi IAM. Synthesis, hypoglycemic and hypolipidemic activities of novel thiazolidinedione derivatives containing thiazole/triazole/oxadiazole ring. Eur J Med Chem 2012; 53: 308-15.
[http://dx.doi.org/10.1016/j.ejmech.2012.04.015] [PMID: 22575535]
[63]
Karrouchi K, Radi S, Ansar M, Taoufik J, Ghabbour HA, Mabkhot YN. Crystal structure of N′-(4-nitrobenzylidene)-5- phenyl-1H-pyrazole-3-carbohydrazide, C17H13N5O3. Z Kristallogr New Cryst Struct 2016; 231(3): 839-41.
[http://dx.doi.org/10.1515/ncrs-2015-0287]
[64]
Nossier ES, Fahmy HH, Khalifa NM, El-Eraky WI, Baset MA. Design and Synthesis of novel Pyrazole-substituted different nitrogenous heterocyclic ring systems as potential anti-inflammatory agents. Molecules 2017; 22(4): 1-16.
[http://dx.doi.org/10.3390/molecules22040512] [PMID: 28338602]
[65]
Lv XH, Ren ZL, Zhou BG, et al. Discovery of N-(benzyloxy)-1,3-diphenyl-1H-pyrazole-4-carboxamide derivatives as potential antiproliferative agents by inhibiting MEK. Bioorg Med Chem 2016; 24(19): 4652-9.
[http://dx.doi.org/10.1016/j.bmc.2016.08.002] [PMID: 27515719]
[66]
Kumar P, Duhan M, Kadyan K, Sindhu J, Kumar S, Sharma H. Synthesis of novel inhibitors of α-amylase based on the thiazolidine-4-one skeleton containing a pyrazole moiety and their configurational studies. MedChemComm 2017; 8(7): 1468-76.
[http://dx.doi.org/10.1039/C7MD00080D] [PMID: 30108858]
[67]
Khan M, Alam A, Khan KM, et al. Flurbiprofen derivatives as novel α-amylase inhibitors: Biology-oriented drug synthesis (BIODS), in vitro, and in silico evaluation. Bioorg Chem 2018; 81: 157-67.
[http://dx.doi.org/10.1016/j.bioorg.2018.07.038] [PMID: 30125730]
[68]
Adegboye AA, Khan KM, Salar U, et al. 2-Aryl benzimidazoles: Synthesis, In vitro α-amylase inhibitory activity, and molecular docking study. Eur J Med Chem 2018; 150: 248-60.
[http://dx.doi.org/10.1016/j.ejmech.2018.03.011] [PMID: 29533872]
[69]
Javid MT, Rahim F, Taha M, et al. Synthesis, in vitro α-glucosidase inhibitory potential and molecular docking study of thiadiazole analogs. Bioorg Chem 2018; 78: 201-9.
[http://dx.doi.org/10.1016/j.bioorg.2018.03.022] [PMID: 29597114]
[70]
Gollapalli M, Taha M, Ullah H, et al. Synthesis of Bis-indolylmethane sulfonohydrazides derivatives as potent α-Glucosidase inhibitors. Bioorg Chem 2018; 80: 112-20.
[http://dx.doi.org/10.1016/j.bioorg.2018.06.001] [PMID: 29894890]
[71]
Naureen S, Chaudhry F, Munawar MA, Ashraf M, Hamid S, Khan MA. Biological evaluation of new imidazole derivatives tethered with indole moiety as potent α-glucosidase inhibitors. Bioorg Chem 2018; 76: 365-9.
[http://dx.doi.org/10.1016/j.bioorg.2017.12.014] [PMID: 29232634]
[72]
Taha M, Imran S, Rahim F, Wadood A, Khan KM. Oxindole based oxadiazole hybrid analogs: Novel α-glucosidase inhibitors. Bioorg Chem 2018; 76: 273-80.
[http://dx.doi.org/10.1016/j.bioorg.2017.12.001] [PMID: 29223804]
[73]
Taha M, Baharudin MS, Ismail NH, et al. Synthesis, α-amylase inhibitory potential and molecular docking study of indole derivatives. Bioorg Chem 2018; 80: 36-42.
[http://dx.doi.org/10.1016/j.bioorg.2018.05.021] [PMID: 29864686]
[74]
Deighton N, Brennan R, Finn C, Davis HV. Antioxidant properties of domesticated and wild Rubus species. J Sci Food Agric 2000; 80: 1307-13.
[http://dx.doi.org/10.1002/1097-0010(200007)80:9<1307:AID-JSFA638>3.0.CO;2-P]
[75]
Kahkonen MP, Heinamaki J, Ollilainen V, Heinonen M. Berry anthocyanins: isolation, identification and antioxidant activities. J Sci Food Agric 2003; 83: 1403-11.
[http://dx.doi.org/10.1002/jsfa.1511]
[76]
Block G, Patterson B, Subar A. Fruit, vegetables, and cancer prevention: A review of the epidemiological evidence. Nutr Cancer 1992; 18(1): 1-29.
[http://dx.doi.org/10.1080/01635589209514201] [PMID: 1408943]
[77]
Yochum L, Kushi LH, Meyer K, Folsom AR. Dietary flavonoid intake and risk of cardiovascular disease in postmenopausal women. Am J Epidemiol 1999; 149(10): 943-9.
[http://dx.doi.org/10.1093/oxfordjournals.aje.a009738] [PMID: 10342803]
[78]
Broadhurst CL, Polansky MM, Anderson RA. Insulin-like biological activity of culinary and medicinal plant aqueous extracts in vitro. J Agric Food Chem 2000; 48(3): 849-52.
[http://dx.doi.org/10.1021/jf9904517] [PMID: 10725162]
[79]
McDougall GJ, Shpiro F, Dobson P, Smith P, Blake A, Stewart D. Different polyphenolic components of soft fruits inhibit alpha-amylase and alpha-glucosidase. J Agric Food Chem 2005; 53(7): 2760-6.
[http://dx.doi.org/10.1021/jf0489926] [PMID: 15796622]
[80]
Ashok Kumar BS, Lakshman K, Nandeesh R, et al. In vitro alpha-amylase inhibition and in vivo antioxidant potential of Amaranthus spinosus in alloxan-induced oxidative stress in diabetic rats. Saudi J Biol Sci 2011; 18(1): 1-5.
[http://dx.doi.org/10.1016/j.sjbs.2010.08.002] [PMID: 23961097]
[81]
Yilmazer-Musa M, Griffith AM, Michels AJ, Schneider E, Frei B. Inhibition of alpha-amylase and alpha-glucosidase activity by tea and grape seed extracts and their constituent catechins. J Agric Food Chem 2012; 60(36): 8924-9.
[http://dx.doi.org/10.1021/jf301147n] [PMID: 22697360]
[82]
Narkhede MB. Evaluation of alpha-amyalse inhibitory potential of four traditional culinary leaves. Asian J Pharm Clin Res 2012; 5: 75-6.
[83]
Salehi P, Asghari B, Esmaeili MA, Dehghan H, Ghazi I. Alpha-glucosidase and alpha-amylase inhibitory effect and antioxidant activity of ten plant extracts traditionally used in Iran for diabetes. J Med Plants Res 2013; 7(6): 257-66.
[84]
Nair SS, Kavrekar V, Mishra A. In vitro studies on alpha-amylase and alpha-glucosidase inhibitory activities of selected plant extracts. J Exp Biol 2013; 3(1): 128-32.
[85]
Sales PM, Souza PM, Simeoni LA, Silveira D. α-Amylase inhibitors: A review of raw material and isolated compounds from plant source. J Pharm Pharm Sci 2012; 15(1): 141-83.
[http://dx.doi.org/10.18433/J35S3K] [PMID: 22365095]
[86]
Jyothi KSN, Shailaja M, Viveni J, Suresh C. Identification of a proteinaceous alpha-amylase inhibitor from a medicinal herb Oxalis corniculata L. (Oxalidaceae). J Homeop Ayurv Med 2014; 3(4): 1-5.
[87]
Elya B, Handayani R, Sauriasari R, Azizahwati Hasyyati US, Permana ID, Permatasari YI. Antidiabetic activity and phytochemical screening of extracts from Indonesian plants by inhibition of alpha-amylase, alpha- glucosidase and dipeptidyl peptidase IV. Pak J Biol Sci 2015; 18(6): 279-84.
[http://dx.doi.org/10.3923/pjbs.2015.279.284]
[88]
Sheliya MA, Begum R, Pillai KK, et al. In vitro alpha-glucosidase and alpha-amylase inhibition by aqueous, hydroalcoholic, and alcoholic extract of Euphorbia hirta L. Drug Dev Ther 2016; 7: 26-30.
[http://dx.doi.org/10.4103/2394-6555.180156]
[89]
Chauhan S, Kaur A, Vyas M, Khatik GL. Comparison of antidiabetic and antioxidant activity of wild and and cultivated variety of Rauwolfia Serpentina. Asian J Pharm Clin Res 2017; 10(12): 404-6.
[http://dx.doi.org/10.22159/ajpcr.2017.v10i12.21287]
[90]
Gajbhiye RL, Ganapathy A, Jaisankar P. A review of alpha-glucosidase and alpha-amylase inhibitors for type 2 diabetes isolated from some important Indian medicinal plants. Ann Clin Pharmacol Ther 2018; 1(1): 1-10.

Rights & Permissions Print Cite
Article Metrics
44
1
© 2024 Bentham Science Publishers | Privacy Policy