Potent Natural Inhibitors of Alpha-Glucosidase and the Application of Aspergillus spp. in Diabetes type 2 Drugs: a Review

Diabetes Mellitus has been becoming a disease of the century, and incidence is still rising worldwide. It causes many serious complications, especially in eye, heart, kidneys, brain, vascular system, such as diabetic nephropathy, retinopathy, liver fa­ilure, etc. Moreover, process controlling this complicated. Meanwhile, antidiabetic drugs on market are facing some problems with wide range adverse reactions. Therefore, finding new to treat diabetes always topic that researchers interested in, derived from nature like microorganisms medicinal plants. This review provide knowledge concerning effects α-glucosidase inhibitors, which oral commonly used for mellitus type 2. Besides, we show readers variety active ingredients originating nature, particularly secondary metabolites Aspergillus spp., have applications chemical industry.
 Keywords:
 Diabetes, Aspergillus.
 References
 [1] W. H. Organization, Classification Mellitus, https://www.who.int/westernpacific/health-topics/diabetes (accessed on: May 11th, 2021).[2] J. Thrasher, Pharmacologic Management Type 2 Mellitus: Available Therapies, Am J Cardiol, Vol. 120, No. 1, 2017, pp. S4-S16, https://doi.org/10.1016/j.amjcard.2017.05.009.[3] Hakamata, M. Kurihara, Okuda, T. Nishio, Oku, Design Screening Strategies Alpha-glucosidase Inhibitors Based Enzymological Information, Curr Top Med Chem, 9, 2009, 3-12, https://doi.org/10.2174/156802609787354306.[4] US, Patent Version Number: US4062950A, Amino Sugar Derivatives, https://patents.google.com/patent/US4062950A/en(accessed 2021).[5] A. S. Dabhi, N. R. Bhatt, Shah, Voglibose: an Alpha- glucosidase Inhibitor, Clin Diagn Res, 7, 12, 2013, 3023-3027, https://doi.org/10.7860/JCDR/2013/6373.3838.[6] P. Durruty, Sanzana, L. Sanhueza, Pathogenesis - Pathophysiology Modern Management, Intechopen, United Kingdom, 2019, 1-18.[7] Khue, Dang, Quang, Khue et al., Guidelines Diagnosis Treatment 2, Ministry Health, Vietnam, 2021 (in Vietnamese).[8] Okuyama, Saburi, Mori, Kimura, Alpha-Glucosidases Alpha-1,4-Glucan Lyases: Structures, Functions, Physiological Actions, Cell Mol Life Sci, 73, 2016, 2727-2751, https://doi.org/10.1007/s00018-016-2247-5.[9] V. Yip, G. Withers, Nature's Many Mechanisms The Degradation Oligosaccharides, Org Biomol 19, 2004, 2707-2713, https://doi.org/10.1039/B408880H.[10] B. Henrissat, Bairoch, New Families Glycosyl Hydrolases Acid Sequence Similarities, Biochem J, 293, 3, 1993, 781-788, https://doi.org/10.1042/bj2930781.[11] A 280, 1991, 309-316, https://doi.org/10.1042/bj2800309.[12] Gupta, Gigras, Mohapatra, K. Goswami, Chauhan, Microbial A-amylases: Biotechnological Perspective, Process Biochemistry, 38, 11, 2003, 1599-1616, https://doi.org/10.1016/s0032-9592(03)00053-0.[13] C. D. Maarel, Veen, C .M. Uitdehaag, Leemhuis, Dijkhuizen, Properties Applications Starch-Converting Enzymes A-Amylase Family, Journal Biotechnology, 94, 2002, 137-155, https://doi.org/10.1016/s0168-1656(01)00407-2.[14] Kim, Jeong, Ko, Shim, Characterization Novel Thermophilic Alpha-Glucosidase Bifidobacterium Longum, Int Biol Macromol, 99, 594-599, https://doi.org/10.1016/j.ijbiomac.2017.03.009.[15] Rose, Chaudet, Jones, Structural Studies Intestinal Alpha-Glucosidases, Maltase-glucoamylase Sucrase-isomaltase, Pediatr Gastroenterol Nutr, 66, 2018, S11-S13, https://doi.org/10.1097/MPG.0000000000001953.[16] Ren, X. Qin, Cao, Wang, F. Bai, Y. Shen, Insight into Substrate Specificity Human Maltase-Glucoamylase, Protein Cell, 2011, 827-836, https://doi.org/10.1007/s13238-011-1105-3.[17] Sim, Willemsma, Mohan, Naim, Pinto, Basis Selectivity Maltase-Glucoamylase Sucrase-Isomaltase N-Terminal Domains, 285, 23, 2010, 17763-17770, https://doi.org/10.1074/jbc.M109.078980.[18] Kumarasamy,H. Liu, Avery, Q. Calvillo, Nichols, Mapping Alpha-Glucogenic Enzyme Specificities Starch Digesting Mal se-Glucoamylase Sucrase-Isomaltase, Bioorg 3929-3934, https://doi.org/10.1016/j.bmc.2011.05.033.[19] Chau, Nghia, Application, Education Publisher, 2009.[20] Researchgate, Food Protein-Derived Bioactive Peptides Scientific Figure, https://www.researchgate.net/figure/Mechanism-of-action-of-alpha-glucosidase-inhibitors_fig2_279991207 10th, 2021).[21] Z. Ma, Recent Advances Synthetic Inhibitors, Chem 819-829, https://doi.org/10.1002/cmdc.201700216.[22] Lee, Patrick, Wishart, Horowitz, E. Morley, Effects Miglitol Glucagon-Like Peptide-1 Secretion And Appetite Sensations Obese Diabetics, Obes Metab, 4, 5, 329-335, https://doi.org/10.1046/j.14631326.2002.00219.x.[23] I. Takei, Miyamoto, O. Funae, Ohashi, Meguro, Tokui, Saruta, GIP Responders Acarbose (NIDDM) Patients, Its Complications, 15, 2001, 245-249, https://doi.org/10.1016/s1056-8727(01)00148-9.[24] Bian, Fan, Ke, Luan, Zhao, Zeng, Synthesis Inhibitory Activity Evaluation N-Substituted Aminomethyl-Beta-D-Glucopyranosides, 21, 17, 5442-5450, https://doi.org/10.1016/j.bmc.2013.06.002.[25] Yang, Tian, Dai, Ye, α-Glucosidase Extracted Roots Polygonum Multiflorum Thunb, Fitoterapia, 117, 65-70, https://doi.org/10.1016/j.fitote.2016.11.009.[26] Yin, Zhang, Feng, Kang, Isolated Medicinal Plants, Science Wellness, No.3-4, 2014, 136-174, https://doi.org/10.1016/j.fshw.2014.11.003.[27] Qiu, Chen, Cai, She, Secondary Metabolites Mangrove Fungus Mycosphaerella sp. SYSU-DZG01, Mar Drugs, 8, 483-508, https://doi.org/10.3390/md17080483.[28] Munasaroh, Tamat, Dewi, Isolation Identification Inhibitor Terreus F38, Indonesian Pharmacy, 29, 74-79, https://doi.org/10.14499/indonesianjpharm29iss2pp74.[29] Suparman, Mulyani, Lotulung, Compound Aculeatus, Annales Bogorienses, 20, 19-23, https://doi.org/10.14203/ann. bogor .2016.v20.n1.19-23.[30] Tachibana, Darmawan, Effect Inhibition Antioxidant Activities Butyrolactone Derivatives MC751, Chemistry Research, 454-460, https://doi.org/10.1007/s00044-013-0659-4.[31] Yi, Production Peptide Oryzae N159-1, Mycobiology, 41, 149-154, https://doi.org/10.5941/MYCO.2013.41.3.149.[32] Onose, Ikeda, Nakagawa, Yamagishi, Higuchi, Miyazawa, Alpha-Glycosidase 1-Deoxynojirimycin Bacillus Species, 138, 516-523, https://doi.org/10.1016/j.foodchem.2012.11.012.[33] Zhu, Yamaki, Yoshihashi, Ohnishi Kameyama, Li, Cheng, Purification (DNJ) Okara Fermented by Subtilis B2 Chinese Traditional (Meitaoza), Agric 58,No. 4097-4103, https://doi.org/10.1021/jf9032377.[34] Tabussum, Riaz, Saleem, Ashraf, Ahmad, U. Alam, Jabeen, Malik, Jabbar, Constituents Chrozophora Plicata, Phytochemistry Letters, 6, 4. 614-619, https://doi.org/10.1016/j.phytol.2013.08.005.[35] Yagi, Kouno, Aoyagi, Murai, Structure Moranoline, Piperidine Alkaloid Morus Agricultural Chemical Society Japan, 50, 1976, 571-572, https://doi.org/10.1271/nogeikagaku1924.50.11_571.[36] Hemker, Stratmann, Goeke, Schroder, Lenz, Piepersberg, Pape, Identification, Cloning, Expression, Extracellular Acarbose-Modifying Glycosyltransferase, AcbD, Actinoplanes Sp. Strain SE50, Bacteriol, 183, 4484-4492, https://doi.org/10.1128/JB.183. 15.4484-4492.2001.[37] Truscheit, Hillebrand, Junge, Müller, Puls, Schmidt, Inhibitors: Chemistry, Therapeutic Potential, Presented at Drug Concentration Monitoring alpha-Glucosidase Plasminogen Activators, Springer-Verlag, Berlin, 1988.[38] Kameda, Asano, Yoshikawa, Takeuchi, Yamaguchi, Matsui, Horii, Fukase, Valiolamine, Inhibiting Aminocyclitol Produced Streptomyces Hygroscopicus, Antibiot (Tokyo), 37, 1984, 1301-1307, https://doi.org/10.7164/antibiotics.37.1301.[39] Tuyen, Hanh, Hang, Trinh, Quyen, Extraction DNJ (1-Deoxynojirimycin) VN9 National Biotechnology Conference, 2013.[40] Optimization YT20 Vietnam Technology, 59, 2021, 179-188, https://doi.org/10.15625/2525-2518/ 59/2/14928.[41] Baker, Bennett, An Overview Genus Aspergillus, Aspergillus: Molecular Biology Genomics, Aspergilli, Taylor & Francis, 2008, 3-13.[42] Gugnani, Ecology Taxonomy Pathogenic Front Biosci, s346- s357, https://doi.org/10.2741/1002.[43] Shaw, Science, 150, 3697, 1965, 736-737, https://doi.org/10.1126/science.150.3697.736-a.[44] Hedayati, Pasqualotto, Warn, Bowyer, Denning, Flavus: Pathogen, Allergen Mycotoxin Producer, Microbiology, 153, 2007, 1677-1692, https://doi.org/10.1099/mic.0.2007/007641-0.[45] Dagenais, Keller, Fumigatus Invasive Aspergillosis, Microbiol Rev, 22, 447-465, https://doi.org/10.1128/CMR.00055-08.[46] Amaike, Flavus, Annu Rev Phytopathol, 49, 107-133, https://doi.org/10.1146/annurev-phyto-072910-095221.[47] Houbraken, De Vries, Samson, Biotechnologically Important Penicillium Adv Appl Microbiol, 86, 199-249, https://doi.org/10.1016/B978-0-12-800262-9.00004-4.[48] Ichishima, Development Technology Oryzae, Sojae, Luchuensis, Microorganisms Biosci Biotechnol Biochem, 80, 1681-1692, https://doi.org/10.1080/09168451.2016.1177445.[49] Schuster, Dunn-Coleman, Frisvad, Van Dijck, Safety Niger-A Review, Biotechnol, 4-5, 426-435, https://doi.org/10.1007/s00253-002-1032-6.[50] Yu, Regulation Metabolism Filamentous Fungi, 43, 2005, 437-458, https://doi.org/10.1146/annurev.phyto.43.040204.140214.[51] Sanchez, Somoza, Metabolite Research Post-Genomic Era, Nat Prod Rep, 2012, 351-371, https://doi.org/10.1039/c2np00084a.[52] Klich, Mycotoxins, 16, 497-516, https://doi.org/10.1128/cmr.16.3.497-516.2003.[53] Zhou, Liao, Statins cardiovascular Diseases: Cholesterol Lowering Pleiotropy, Pharm Des, 467-478, https://doi.org/10.2174/138161209787315684.[54] Alberts, Discovery, Biochemistry Lovastatin, 62, 1988, 10J-15J, https://doi.org/10.1016/0002-9149(88)90002-1.[55] Tomoda, Nishida, Masuma, Omura, Pyripyropenes, Acyl-Coa: Acyltransferase Fumigatu- Production, Isolation, Biological Properties, 47, 1994, 148-153, https://doi.org/10.7164/antibiotics.47.148.[56] Pelaez, Fungal Metabolites, Marcel Dekker, Stated America, 2004.[57] Dulaney, Penicillin Nidulans Group, Mycologia, 39, 582-586, https://doi.org/10.1080/00275514.1947.12017637.[58] Bladt, Knudsen, Larsen, Anticancer Antifungal Compounds Other Molecules, 18, 11338-11376, https://doi.org/10.3390/molecules180911338.[59] Wu, Huang, Pan, Yan, Diphenyl Ethers Phenolic Bisabolane Sesquiterpenoids Endophytic Flavus QQSG-3, 307-316, https://doi.org/10.3390/md16090307.