Author(s): Shakeel Ahmed Ansari, Fatma El-Sayed Hassan, Asim Muhammed Alshanberi, Mohammed Shaikhomer, Rukhsana Satar

Email(s): shakeel.ansari@bmc.edu.sa

DOI: 10.52711/0974-360X.2026.00691   

Address: Shakeel Ahmed Ansari1*, Fatma El-Sayed Hassan2,3, Asim Muhammed Alshanberi2, Mohammed Shaikhomer2,4, Rukhsana Satar5
1Department of Biochemistry, General Medicine Practice Program, Batterjee Medical College, Jeddah 21442, Saudi Arabia.
2General Medicine Practice Program, Batterjee Medical College, Jeddah 21442, Saudi Arabia.
3Medical Physiology Department, Kasr Alainy, Faculty of Medicine, Cairo University, Giza 11562, Egypt.
4Department of Internal Medicine, Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia.
5Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
*Corresponding Author

Published In:   Volume - 19,      Issue - 10,     Year - 2026


ABSTRACT:
Since a-amylase is essential for the metabolism of carbohydrates, its inhibition could be a useful treatment approach for controlling hyperglycemia. The aim of this review is to analyze the biological mechanisms of a-amylase inhibitors (a-AIs) and their consequences for managing hyperglycemia. A thorough search of literature was done utilizing several databases, including Google Scholar, PubMed, and Scopus. Peer-reviewed research articles, clinical trials, and reviews written in English were included. The involved studies were discussing the origin, structure, and the impact of both natural and artificial a-AIs, emphasizing those generated by plants and microbes. The a-AIs mitigates the health risks linked to hyperglycemia by slowing down the breakdown of carbohydrates, lowering postprandial glucose surges, and therefore enhancing glycemic control. When compared to their synthetic counterparts, such as acarbose and miglitol, natural inhibitors, such as flavonoids and saponins from plants, typically have less adverse effects. Synthetic and natural a-AIs are an intriguing approach to treat hyperglycemia. Investigating a-AIs further, focusing on discovering novel a-AIs that exhibit much better effectiveness and reduced side effects, refining combination treatments, and tailoring care according to patient characteristics may result in novel approaches to hyperglycemia treatment, which would eventually benefit patients.


Cite this article:
Shakeel Ahmed Ansari, Fatma El-Sayed Hassan, Asim Muhammed Alshanberi, Mohammed Shaikhomer, Rukhsana Satar. Therapeutic Potential of α-amylase Inhibitors in Managing Hyperglycemia. Research Journal Pharmacy and Technology. 2026;19(10):4963-0. doi: 10.52711/0974-360X.2026.00691

Cite(Electronic):
Shakeel Ahmed Ansari, Fatma El-Sayed Hassan, Asim Muhammed Alshanberi, Mohammed Shaikhomer, Rukhsana Satar. Therapeutic Potential of α-amylase Inhibitors in Managing Hyperglycemia. Research Journal Pharmacy and Technology. 2026;19(10):4963-0. doi: 10.52711/0974-360X.2026.00691   Available on: https://rjptonline.org/AbstractView.aspx?PID=2026-19-10-67


REFERENCES:
1.    Suwała S, Junik R. Hyperglycemia as the Most Important Risk Factor for Serum Hypomagnesemia in Metabolic Syndrome. Diabetology. 2025; 6: 82-86. 
2.    Alabdali MM, Alrasheed AS, Alghirash FA, et al. Stress Hyperglycemia as a Prognostic Indicator of the Clinical Outcomes in Patients with Stroke: A Comprehensive Literature Review. Biomedicines. 2025; 13: 1834-1840.
3.    Nițulescu IM, Ciulei G, Cozma A, et al. From Innate Immunity to Metabolic Disorder: A Review of the NLRP3 Inflammasome in Diabetes Mellitus. J Clin Med. 2023; 12(18): 6022-6030.
4.    Lovic D, Piperidou A, Zografou I, Grassos H, et al. The Growing Epidemic of Diabetes Mellitus. Curr Vasc Pharmacol. 2020;18(2):104-109.
5.    Taylor SI, Yazdi ZS, Beitelshees AL. Pharmacological treatment of hyperglycemia in type 2 diabetes. J Clin Invest. 2021; 131(2): e142243-51. 
6.    Hamblin PS, Russell AW, Talic S, et al. The growing range of complications of diabetes mellitus. Trends Endocrinol Metab. 2025 Jan 3: S1043-2760(24)00328. 
7.    Agrawal N, Sharma M, Singh S, et al. Recent Advances of α-Glucosidase Inhibitors: A Comprehensive Review. Curr Top Med Chem. 2022; 22(25): 2069-2086. 
8.    Han X, Wang P, Zhang J, et al. α-Glucosidase Inhibition Mechanism and Anti-Hyperglycemic Effects of Flavonoids from Astragali Radix and Their Mixture Effects. Research Journal of Pharmacy and Technology. 2026;19(2):1-8. 
9.    S. Singh, S. Patni, A. Singh, et al. α-Amylase Inhibitors: A Safe Nutraceutical Approach for Obesity Management. Nutraceuticals in Obesity Management and Control. 2025;353-378. 
10.    Li W, Yang S, An J, et al. Statistical Characterization of Food-Derived α-Amylase Inhibitory Peptides: Computer Simulation and Partial Least Squares Regression Analysis. Molecules. 2024 Jan 13;29(2):395-401. 
11.    Li X, Bai Y, Jin Z, et al. Food-derived non-phenolic α-amylase and α-glucosidase inhibitors for controlling starch digestion rate and guiding diabetes-friendly recipes. LWT. 2022; 153: 112455-112461.
12.    Masson P, Mukhametgalieva AR. Partial Reversible Inhibition of Enzymes and Its Metabolic and Pharmaco-Toxicological Implications. Int. J. Mol. Sci. 2023; 24: 12973-12980.
13.    Mahmood N. A review of α-amylase inhibitors on weight loss and glycemic control in pathological state such as obesity and diabetes. Comp Clin Pathol. 2016; 25: 1253-1264.
14.    Kashtoh H, Baek KH. New Insights into the Latest Advancement in α-Amylase Inhibitors of Plant Origin with Anti-Diabetic Effects. Plants (Basel). 2023;12:125-133.
15.    Ali M, Hassan M, Ansari SA, et al. Quercetin and Kaempferol as Multi-Targeting Antidiabetic Agents against Mouse Model of Chemically Induced Type 2 Diabetes. Pharmaceuticals (Basel). 2024; 17: 61-66.
16.    Zhang J. α-Amylase inhibition of a certain dietary polyphenol is predominantly affected by the concentration of α-1, 4-glucosidic bonds in starchy and artificial substrates. Food Res Int. 2022; 157: 111210.
17.    El Hazzam K, Mhada M, Ben Bakrim W, et al. Antinutritional and insecticidal potential of Chenopodium quinoa saponin rich extract against Tribolium castaneum (Herbst) and its action mechanism. Sci Rep. 2025; 15: 6829-6836.
18.    Lo Piparo E, Scheib H, Frei N, et al. Flavonoids for controlling starch digestion: structural requirements for inhibiting human alpha-amylase. J Med Chem. 2008; 51: 3555-3561.
19.    Najafian M, Ebrahim-Habibi A, Hezareh N, et al. Trans-chalcone: a novel small molecule inhibitor of mammalian alpha-amylase. Mol Biol Rep. 2011; 38: 1617-1620.
20.    Okokon JE, Etuk IC, Thomas PS, et al. In vivo antihyperglycaemic and antihyperlipidemic activities and chemical constituents of Solanum anomalum. Biomed Pharmacother. 2022; 151: 1131-1142.
21.    Daoudi NE, Bouhrim M, Ouassaou H, et al. Inhibitory effect of roasted/unroasted Argania spinosa seeds oil on α-glucosidase, α-amylase and intestinal glucose absorption activities. South African J Bot. 2020; 135: 413-420.
22.    Quek A, Kassim NK, Ismail A, et al. Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from Melicope glabra (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods. Molecules. 2021; 26: 1-7.
23.    Tekulu GH, Araya EM, Mengesha HG. In vitro α-amylase inhibitory effect of TLC isolates of Aloe megalacantha baker and Aloe monticola Reynolds. BMC Complement Altern Med. 2019; 19: 206-211.
24.    Panigrahy SK, Kumar A, Bhatt R. Hedychium coronarium Rhizomes: Promising Antidiabetic and Natural Inhibitor of α-Amylase and α-Glucosidase. J Diet Suppl. 2020; 17(1): 81-87.
25.    Hawash M, Jaradat N, Elaraj J, et al. Antidiabetic effect of seven plants from Palestine. J Complement Integr Med. 2020;17(1):20190032-41.
26.    Sansenya S, Payaka A, Wannasut W, et al. Biological activity of rice extract and the inhibition potential of rice extract, rice volatile compounds and their combination against α-glucosidase, α-amylase and tyrosinase. Int J Food Sci Technol. 2020; 56(4): 1865-1876.
27.    Xu S, Qin L, Mazhar M, et al. Functional components profile and glycemic index of kidney beans. Front Nutr. 2022; 9: 1044427-36.
28.    Quek A, Kassim NK, Lim PC, et al. α-Amylase and dipeptidyl peptidase-4 (DPP-4) inhibitory effects of Melicope latifolia bark extracts and identification of bioactive constituents using in vitro and in silico approaches. Pharm Biol. 2021; 59(1): 964-973.
29.    Sani D, Munna A, Salim M, et al. Evaluation of α-amylase Inhibition and Cytotoxic Activities of the Arachis hypogaea and Cinnamomum tamala. Curr Nutr Food Sci. 2020; 17: 328-336.
30.    Romero Rocamora C, Ramasamy K, Meng Lim S, et al. HPTLC based approach for bioassay-guided evaluation of antidiabetic and neuroprotective effects of eight essential oils of the Lamiaceae family plants. J Pharm Biomed Anal. 2020; 178: 112909-12.
31.    Wu M, Yang Q, Wu Y, et al. Inhibitory effects of acorn (Quercus variabilis Blume) kernel-derived polyphenols on the activities of α-amylase, α-glucosidase, and dipeptidyl peptidase IV. Food Biosci. 2021; 43: 101224-32.
32.    Sen A, Mine K, Baser KHC. Chemical composition, antiradical, and enzyme inhibitory potential of essential oil obtained from aerial part of Centaurea pterocaula Trautv. J Essent Oil Res. 2021; 33: 44-52.
33.    Paun G, Neagu E, Albu C, et al. In Vitro Evaluation of Antidiabetic and Anti-Inflammatory Activities of Polyphenolic-Rich Extracts from Anchusa officinalis and Melilotus officinalis. ACS Omega. 2020; 5(22): 13014-13022.
34.    Hoang Anh L, Xuan TD, Dieu Thuy NT, et al. Antioxidant and α-amylase Inhibitory Activities and Phytocompounds of Clausena indica Fruits. Medicines. 2020; 7(3): 10-21.
35.    Mahesh Kumar JG, Nyola NK. In-vitro and in-vivo Anti-Hyperglycemic Potential of Prosopis cineraria Pods Extract and Fractions. J Biol Act Prod Nat. 2019; 9(2): 135-140.
36.    Prasathkumar M, Raja K, Vasanth K, et al. Phytochemical screening and in vitro antibacterial, antioxidant, anti-inflammatory, anti-diabetic, and wound healing attributes of Senna auriculata (L.) Roxb. leaves. Arab. J. Chem. 2021; 14, 103345-56.
37.    Al Ahmed A, Khalil HE. Antidiabetic‎ Activity of Terfezia Claveryi; An In Vitro and In Vivo Study. Biomed Pharmacol J. 2019; 12(2): 603-608.
38.    Prakash V. Determination of α-Amylase Inhibitory Potential of Leaf Extracts of Rhododendron arboreum Sm. and Rhododendron campanulatum. J Drug Deliv Ther. 2022; 12: 2022-31.
39.    Mazumder K, Sumi TS, Golder M, et al. Antidiabetic profiling, cytotoxicity and acute toxicity evaluation of aerial parts of Phragmites karka (Retz.). J Ethnopharmacol. 2021; 270: 113781-90.
40.    da Silva Humberto de Moura Barbosa RL, et al. Hexane fraction from Brazilian Morus nigra leaves improved oral carbohydrate tolerance and inhibits α-amylase and α-glucosidase activities in diabetic mice. Nat Prod Res. 2021; 35(22): 4785-4788.
41.    Ktari N, Salem RBSB, Bkhairia IS, et al. Functional properties and biological activities of peptides from zebra blenny protein hydrolysates fractionated using ultrafiltration. Food Biosci. 2020; 34: 100539-46.
42.    Renganathan S, Manokaran S, Vasanthakumar P, et al. Phytochemical Profiling in Conjunction with In Vitro and In Silico Studies to Identify Human α-Amylase Inhibitors in Leucaena leucocephala (Lam.) De Wit for the Treatment of Diabetes Mellitus. ACS Omega. 2021; 6(29):19045-19057.
43.    Pandey BP, Pradhan SP, Adhikari K, et al. Bergenia pacumbis from Nepal, an astonishing enzymes inhibitor. BMC Complement Med Ther. 2020; 20(1): 198-207.
44.    Jaradat N, Abualhasan MN, Qadi M, et al. Antiamylase, Antilipase, Antimicrobial, and Cytotoxic Activity of Nonea obtusifolia (Willd.) DC. from Palestine. Biomed Res Int. 2020; 2020: 8821319-27.
45.    Jan B, Zahiruddin S, Basist P, et al. Metabolomic Profiling and Identification of Antioxidant and Antidiabetic Compounds from Leaves of Different Varieties of Morus alba Linn Grown in Kashmir. ACS Omega. 2022; 7(28): 24317-24328.
46.    Omar RM, Badria FA, Galala AA. An emerging flavone glycoside from Phyllanthus emblica L.: A promiscuous enzyme inhibitor and potential therapeutic in chronic diseases. South African J Bot. 2023;153:290-296.
47.    Timalsina D, Bhusal D, Devkota HP, et al. α-Amylase Inhibitory Activity of Catunaregam spinosa (Thunb.) Tirveng.: In Vitro and In Silico Studies. Biomed Res Int. 2021; 2021: 4133876-89.
48.    Choudhary N, Prabhakar PK, Khatik GL, et al. Evaluation of Acute toxicity, In-vitro, In-vivo Antidiabetic Potential of the Flavonoid Fraction of the plant Chenopodium album L. Pharmacogn J. 2021; 13(3): 765-779.
49.    Saraswathi K, Bharkawi R, Khusro A, et al. Assessment on in vitro medicinal properties and chemical composition analysis of Solanum virginianum dried fruits. Arab. J. Chem. 2021; 14(12): 103442-50.
50.    Bello M, Jiddah-kazeem B, Fatoki TH, et al. Antioxidant property of Eucalyptus globulus Labill. extracts and inhibitory activities on carbohydrate metabolizing enzymes related to type-2 diabetes. Biocatal Agric Biotechnol. 2021; 36: 102111-20.
51.    Elsadek MF, Ahmed BM. Effect of sakuranin on carbohydrate-metabolizing enzyme activity modifications in streptozotocin-nicotinamide-induced diabetic wistar rats. Saudi J Biol Sci. 2022; 29(3): 1402-1406.
52.    Hassan A, Khan Mohmand NZ, Ullah H, et al. Antioxidant, Antidiabetic, and Antihypertension Inhibitory Potentials of Phenolic Rich Medicinal Plants. J Chem. 2022; 2022: 1-10. Article ID 9046780.
53.    Remok F, Saidi S, Gourich AA, et al. Phenolic Content, Antioxidant, Antibacterial, Antihyperglycemic, and α-Amylase Inhibitory Activities of Aqueous Extract of Salvia lavandulifolia Vahl. Pharmaceuticals. 2023; 16(3): 395-407.
54.    Karray A, Alonazi M, Jallouli R, et al. A Proteinaceous Alpha-Amylase Inhibitor from Moringa Oleifera Leaf Extract: Purification, Characterization, and Insecticide Effects against C. maculates Insect Larvae. Molecules. 2022; 27(13): 4222-33.
55.    Abolaji OK, Ukwuani-Kwaja AN, Sani I, et al. In-Vitro Antidiabetic Effect of Ziziphus mucronata Leave Extracts. J Drug Deliv Ther. 2021; 11(6-S): 9-13.
56.    Olaokun OO, Manonga SA, Zubair MS, et al. Molecular Docking and Molecular Dynamics Studies of Antidiabetic Phenolic Compound Isolated from Leaf Extract of Englerophytum magalismontanum (Sond.) T.D. Penn. Molecules. 2022;27(10):3175-88.
57.    Yashoda K, Deegendra K, Bimala S. Antioxidant, Ptp 1B Inhibition and Α-Amylase Inhibition Property and Gc-Ms Analysis of Methanolic Leaves Extract of Achyranthes Aspera and Catharanthus Roseus of Nepal. Int J Pharm Pharm Sci. 2021; 13(4): 49-55.
58.    Irfan Dar M, Qureshi MI, Zahiruddin S, et al. In Silico Analysis of PTP1B Inhibitors and TLC-MS Bioautography-Based Identification of Free Radical Scavenging and α-Amylase Inhibitory Compounds from Heartwood Extract of Pterocarpus marsupium. ACS Omega. 2022; 7(50): 46156-46173.
59.    Li F, Luo T, Hou J, et al. Natural α-glucosidase and α-amylase inhibitors from raspberry (Rubus corchorifolius L.) leaf-tea: Screening, identification and molecular docking analysis. LWT. 2023; 181: 114763-72.
60.    Yang Y, Zhang P, Huang Z, et al. Phenolics from Sterculia nobilis Smith pericarp by-products delay carbohydrate digestion by uncompetitively inhibiting α-glucosidase and α-amylase. LWT. 2023; 173: 114339-47.
61.    Kalinovskii AP, Sintsova OV, Gladkikh IN, et al. Natural Inhibitors of Mammalian α-Amylases as Promising Drugs for the Treatment of Metabolic Diseases. Int J Mol Sci. 2023; 24(22): 16514-22.
62.    Saini P, Gangwar M. Inhibition spectrum, purification and kinetic study of alpha-amylase inhibitor from Murraya koenigii endophytic actinobacterium (Streptomyces koyangensis strain B025). Curr Sci. 2018; 115(3): 393-395.
63.    Dat TTH, Oanh PTT. In vitro antioxidant, α-amylase and α-glucosidase inhibitory activities of endophytic bacteria from the roots of the mangrove plant Rhizophora stylosa Griffith. Acad J. 2021; 43: 125-135.
64.    Chandrasekhar C, Rajpurohit H, Javaji K, et al. Anti-hyperglycemic and genotoxic studies of 1-O-methyl chrysophanol, a new anthraquinone isolated from Amycolatopsis thermoflava strain SFMA-103. Drug Chem Toxicol. 2021; 44(2): 148-160.
65.    Indupalli M, Muvva V, Mangamuri U, et al. Bioactive compounds from mangrove-derived rare actinobacterium Saccharomonospora oceani VJDS-3. 3 Biotech. 2018; 8(2): 103-111.
66.    Dat TTH, Cuong LCV, Nhung NTA. The study on biological activity and molecular docking of secondary metabolites from Bacillus sp. isolated from the mangrove plant Rhizophora apiculata Blume. Reg. Stud. Mar. Sci. 2022; 55(4): 102583-94. 
67.    Gulnaz A, Nadeem J, Han JH, et al. Lactobacillus Sps in Reducing the Risk of Diabetes in High-Fat Diet-Induced Diabetic Mice by Modulating the Gut Microbiome and Inhibiting Key Digestive Enzymes Associated with Diabetes. Biology (Basel). 2021; 10(4): 348-359.
68.    Pujiyanto S, Resdiani M, Raharja B, et al. α-Amylase inhibitor activity of endophytic bacteria isolated from Annona muricata L. J Phys Conf Ser. 2018; 1025: 012085.
69.    Ruzieva D, Gulyamova T, Nasmetova S, et al. Identification of Bioactive Compounds of the Endophytic Fungus Aspergillus egypticus-HT166S Inhibiting the Activity of Pancreatic α-Amylase. Turk J Pharm Sci. 2022; 19(6): 630-635.
70.    Khan R, Naqvi STQ, Fatima N, et al. Study of antidiabetic activities of endophytic fungi isolated from plants. Pure Appl Biol. 2019; 8(2): 1287-1295.
71.    Siregar PI, Pujiyanto S, Lunggani AT. Inhibitory activity of endophytic fungi against alpha-amylase isolated from raru (Cotylelobium melanoxylon). Berk Penelit Hayati. 2022; 28(1): 44-50.
72.    Qiu P, Liu Z, Chen Y, et al. Secondary Metabolites with α-Glucosidase Inhibitory Activity from the Mangrove Fungus Mycosphaerella sp. SYSU-DZG01. Mar Drugs. 2019; 17(8): 483-493.
73.    Tamboli E, Bhatnagar A, Mishra A. Alpha-amylase inhibitors from mycelium of an oyster mushroom. Prep Biochem Biotechnol. 2018;48(8):693-699.
74.    Kumar RV, Sinha VR. Newer insights into the drug delivery approaches of α-glucosidase inhibitors. Expert Opin Drug Deliv. 2012; 9(4): 403-416.
75.    Stojkovic D, Ciric A. An insight into antidiabetic properties of six medicinal and edible mushrooms: Inhibition of α-amylase and α-glucosidase linked to type-2 diabetes. South African J Bot. 2019; 120: 100-103.
76.    Saravanakumar K, Sriram B, Sathiyaseelan A, et al. Molecular identification, volatile metabolites profiling, and bioactivities of an indigenous endophytic fungus (Diaporthe sp.). Process Biochem. 2021; 102(7): 72-81. 
77.    Roopa, Madhusudhan M, Nischita R, et al. In vitro studies on anti-diabetic, anti-bacterial and phytochemical activities of endophytic fungal extracts from Salacia species. J Med Plants. 2022; 10(2): 31-37.
78.    Jaber SA. In vitro alpha-amylase and alpha-glucosidase inhibitory activity and in vivo antidiabetic activity of Quercus coccifera (Oak tree) leaves extracts. Saudi J Biol Sci. 2023;30(1):103688-103697.
79.    Gil-Martín E, Forbes-Hernández T, Romero A, et al. Influence of the extraction method on the recovery of bioactive phenolic compounds from food industry by-products. Food Chem. 2022; 378: 131918.
80.    Saleem F, Khan KM, Ullah N, et al. Bioevaluation of synthetic pyridones as dual inhibitors of α-amylase and α-glucosidase enzymes and potential antioxidants. Arch Pharm (Weinheim). 2023; 356(1): e2200400.
81.    Ashok Kumar BS, Lakshman K, Nandeesh R, A 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.
82.    Zinjarde SS, Bhargava SY, Kumar AR. Potent α-amylase inhibitory activity of Indian Ayurvedic medicinal plants. BMC Complement Altern Med. 2011; 11(1): 5-13.
83.    Jiang S, Xu L, Xu Y, et al. Antidiabetic effect of Momordica charantia saponins in rats induced by high-fat diet combined with STZ. Electron J Biotechnol. 2020; 43: 41-47.
84.    Lardinois CK, Greenfield MS, Schwartz HC, et al. Acarbose Treatment of Non-Insulin-Dependent Diabetes Mellitus. Arch Intern Med. 1984; 144(2): 345-347.
85.    Robyt JF. Inhibition, activation, and stabilization of α-amylase family enzymes. Biol Bratislava. 2005; 16: 17-26.
86.    Campbell LK, Baker DE, Campbell RK. Miglitol: Assessment of its role in the treatment of patients with diabetes mellitus. Ann Pharmacother. 2000; 34(11): 1291-1301.
87.    Taira M, Takasu N, Komiya I, et al. Voglibose administration before the evening meal improves nocturnal hypoglycemia in insulin-dependent diabetic patients with intensive insulin therapy. Metabolism. 2000; 49(4): 440-443.
88.    Lee MY, Choi DS, Lee MK, et al. Comparison of acarbose and voglibose in diabetes patients who are inadequately controlled with basal insulin treatment: randomized, parallel, open-label, active-controlled study. J Korean Med Sci. 2014; 29(1): 90-97. 
89.    Al-Asri J, Fazekas E, Lehoczki G, et al. From carbohydrates to drug-like fragments: Rational development of novel α-amylase inhibitors. Bioorg Med Chem. 2015; 23(20): 6725-6732. s

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