<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Current Computer-Aided Drug Design</journal-id><journal-title-group><journal-title xml:lang="en">Current Computer-Aided Drug Design</journal-title><trans-title-group xml:lang="ru"><trans-title>Current Computer-Aided Drug Design</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1573-4099</issn><issn publication-format="electronic">1875-6697</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">644089</article-id><article-id pub-id-type="doi">10.2174/1573409919666230518151414</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Chemistry</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Assessment of Anticholinergic and Antidiabetic Properties of Some Natural and Synthetic Molecules: An In vitro and In silico Approach</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Çomaklı</surname><given-names>Veysel</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Aygül</surname><given-names>İmdat</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Sağlamtaş</surname><given-names>Rüya</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff3"/></contrib><contrib contrib-type="author"><name><surname>Kuzu</surname><given-names>Müslüm</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff4"/></contrib><contrib contrib-type="author"><name><surname>Demirdağ</surname><given-names>Ramazan</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Akincioğlu</surname><given-names>Hülya</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff5"/></contrib><contrib contrib-type="author"><name><surname>Adem</surname><given-names>Şevki</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff6"/></contrib><contrib contrib-type="author"><name><surname>Gülçin</surname><given-names>İlhami</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff7"/></contrib></contrib-group><aff id="aff1"><institution>Department of Nutrition and Dietetics, İbrahim Çeçen University of Ağrı</institution></aff><aff id="aff2"><institution>Department of Nutrition and Dietetics,, Gümüşhane University</institution></aff><aff id="aff3"><institution>Department of Medical Services and Techniques,, İbrahim Çeçen University of Ağrı,</institution></aff><aff id="aff4"><institution>Department of NutritioDepartment of Nutrition and Dieteticsn and Dietetics, Karabük University</institution></aff><aff id="aff5"><institution>Department of Chemistry, İbrahim Çeçen University of Ağrı</institution></aff><aff id="aff6"><institution>Department of Chemistry, Çankırı Karatekin University</institution></aff><aff id="aff7"><institution>Department of Chemistry, Atatürk University</institution></aff><pub-date date-type="pub" iso-8601-date="2024-05-01" publication-format="electronic"><day>01</day><month>05</month><year>2024</year></pub-date><volume>20</volume><issue>5</issue><issue-title xml:lang="ru"/><fpage>441</fpage><lpage>451</lpage><history><date date-type="received" iso-8601-date="2025-01-07"><day>07</day><month>01</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Bentham Science Publishers</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Bentham Science Publishers</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/></permissions><self-uri xlink:href="https://rjeid.com/1573-4099/article/view/644089">https://rjeid.com/1573-4099/article/view/644089</self-uri><abstract xml:lang="en"><p id="idm46041443709360">Introduction:This study aimed to determine the in vitro and in silico effects of some natural and synthetic molecules on acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and α-glucosidase enzymes.</p><p id="idm46041443713360">Background:Alzheimer's disease (AD) and Type II diabetes mellitus (T2DM) are considered the most important diseases of todays world. However, the side effects of therapeutic agents used in both diseases limit their use. Therefore, developing drugs with high therapeutic efficacy and better pharmacological profile is important.</p><p id="idm46041443717328">Objective:This study sets out to determine the related enzyme inhibitors used in treating AD and T2DM, considered amongst the most important diseases of todays world.</p><p id="idm46041443722384">Methods:In the current study, the in vitro and in silico effects of dienestrol, hesperetin, Lthyroxine, 3,3',5-Triiodo-L-thyronine (T3) and dobutamine molecules on AChE, BChE and α- glycosidase enzyme activities were investigated.</p><p id="idm46041443731760">Results:All the molecules showed an inhibitory effect on the enzymes. The IC50 and Ki values of the L-Thyroxine molecule, which showed the strongest inhibition effect for the AChE enzyme, were determined as 1.71 µM and 0.83 ± 0.195 µM, respectively. In addition, dienestrol, T3, and dobutamine molecules showed a more substantial inhibition effect than tacrine. The dobutamine molecule showed the most substantial inhibition effect for the BChE enzyme, and IC50 and Ki values were determined as 1.83 µM and 0.845 ± 0.143 µM, respectively. The IC50 and Ki values for the hesperetin molecule, which showed the strongest inhibition for the α-glycosidase enzyme, were determined as 13.57 µM and 12.33 ± 2.57 µM, respectively.</p><p id="idm46041443739408">Conclusion:According to the results obtained, the molecules used in the study may be considered potential inhibitor candidates for AChE, BChE and α-glycosidase.</p></abstract><kwd-group xml:lang="en"><kwd>Molecular modelling</kwd><kwd>inhibition</kwd><kwd>Alzheimer's disease</kwd><kwd>type II diabetes mellitus</kwd><kwd>acetylcholinesterase</kwd><kwd>butyrylcholinesterase</kwd><kwd>α-glycosidase.</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Friedli, M.J.; Inestrosa, N.C. Huperzine A and its neuroprotective molecular signaling in alzheimers disease. Molecules, 2021, 26(21), 6531. doi: 10.3390/molecules26216531 PMID: 34770940</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Chiang, T.I.; Yu, Y.H.; Lin, C.H.; Lane, H.Y. Novel biomarkers of alzheimers disease: Based upon N-methyl-D-aspartate receptor hypoactivation and oxidative stress. Clin. Psychopharmacol. Neurosci., 2021, 19(3), 423-433. doi: 10.9758/cpn.2021.19.3.423 PMID: 34294612</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Aras, A.; Türkan, F.; Yildiko, U.; Atalar, M.N.; Kılıç, Ö.; Alma, M.H.; Bursal, E. Biochemical constituent, enzyme inhibitory activity, and molecular docking analysis of an endemic plant species, Thymus migricus. Chem. Pap., 2021, 75(3), 1133-1146. doi: 10.1007/s11696-020-01375-z</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Bartolini, M.; Bertucci, C.; Cavrini, V.; Andrisano, V. β-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies. Biochem. Pharmacol., 2003, 65(3), 407-416. doi: 10.1016/S0006-2952(02)01514-9 PMID: 12527333</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Lolak, N.; Akocak, S.; Türkeş, C.; Taslimi, P.; Işık, M.; Beydemir, Ş.; Gülçin, İ.; Durgun, M. Synthesis, characterization, inhibition effects, and molecular docking studies as acetylcholinesterase, α-glycosidase, and carbonic anhydrase inhibitors of novel benzenesulfonamides incorporating 1,3,5-triazine structural motifs. Bioorg. Chem., 2020, 100, 103897. doi: 10.1016/j.bioorg.2020.103897 PMID: 32413628</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Türkan, F.; Huyut, Z.; Taslimi, P.; Gülçin, İ. The effects of some antibiotics from cephalosporin groups on the acetylcholinesterase and butyrylcholinesterase enzymes activities in different tissues of rats. Arch. Physiol. Biochem., 2019, 125(1), 12-18. doi: 10.1080/13813455.2018.1427766 PMID: 29364753</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Benazzouz-Touami, A.; Chouh, A.; Halit, S.; Terrachet-Bouaziz, S.; Makhloufi-Chebli, M.; Ighil-Ahriz, K.; Silva, A.M.S. New Coumarin-Pyrazole hybrids: Synthesis, Docking studies and Biological evaluation as potential cholinesterase inhibitors. J. Mol. Struct., 2022, 1249, 131591. doi: 10.1016/j.molstruc.2021.131591</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Domínguez, R.O.; Pagano, M.A.; Marschoff, E.R.; González, S.E.; Repetto, M.G.; Serra, J.A. Alzheimer disease and cognitive impairment associated with diabetes mellitus type 2: Associations and a hypothesis. Neurología, 2014, 29(9), 567-572. doi: 10.1016/j.nrleng.2014.10.001 PMID: 24140159</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Günsel, A.; Taslimi, P.; Atmaca, G.Y.; Bilgiçli, A.T.; Pişkin, H.; Ceylan, Y.; Erdoğmuş, A.; Yarasir, M.N.; Gülçin, İ. Novel potential metabolic enzymes inhibitor, photosensitizer and antibacterial agents based on water-soluble phthalocyanine bearing imidazole derivative. J. Mol. Struct., 2021, 1237, 130402. doi: 10.1016/j.molstruc.2021.130402</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Deswal, L.; Verma, V.; Devinder, K.; Deswal, Y.; Kumar, A.; Rajnish, K.; Parshad, M.; Bhatia, M. Synthesis, antimicrobial and α-Glucosidase inhibition of new benzimidazole-1,2,3-Triazole-Indoline derivatives: A combined experimental and computational venture. Chem. Pap., 2022, 1, 1-16.</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Gülçin, İ.; Trofimov, B.; Kaya, R.; Taslimi, P.; Sobenina, L.; Schmidt, E.; Petrova, O.; Malysheva, S.; Gusarova, N.; Farzaliyev, V.; Sujayev, A.; Alwasel, S.; Supuran, C.T. Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds  Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and α-glycosidase inhibition properties. Bioorg. Chem., 2020, 103, 104171. doi: 10.1016/j.bioorg.2020.104171 PMID: 32891857</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Gülçin, İ.; Gören, A.C.; Taslimi, P.; Alwasel, S.H.; Kılıc, O.; Bursal, E. Anticholinergic, antidiabetic and antioxidant activities of Anatolian pennyroyal (Mentha pulegium)-analysis of its polyphenol contents by LC-MS/MS. Biocatal. Agric. Biotechnol., 2020, 23, 101441. doi: 10.1016/j.bcab.2019.101441</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Tam, K.Y.; Ju, Y. Pathological mechanisms and therapeutic strategies for Alzheimers disease. Neural Regen. Res., 2022, 17(3), 543-549. doi: 10.4103/1673-5374.320970 PMID: 34380884</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Akocak, S.; Taslimi, P.; Lolak, N.; Işık, M.; Durgun, M.; Budak, Y.; Türkeş, C.; Gülçin, İ.; Beydemir, Ş. Synthesis, characterization, and inhibition study of novel substituted phenylureido sulfaguanidine derivatives as α‐Glycosidase and cholinesterase inhibitors. Chem. Biodivers., 2021, 18(4), e2000958. doi: 10.1002/cbdv.202000958 PMID: 33620128</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Wierzbicka, A.; Mańkowska‐wierzbicka, D.; Cieślewicz, S.; Stelmach‐mardas, M.; Mardas, M. Interventions preventing vaginitis, vaginal atrophy after brachytherapy or radiotherapy due to malignant tumors of the female reproductive organs-a systematic review. Int J Environ Res Public Health., 2021, 18(8), 3932.</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Carraher, C.E., Jr; Roner, M.R.; Shahi, K.; Barot, G. Structural Consideration in designing organotin polyethers to arrest the growth of breast cancer cells In vitro. Materials, 2011, 4(4), 801-815. doi: 10.3390/ma4040801 PMID: 28879951</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Hong, X.; Luo, X.; Wang, L.; Gong, D.; Zhang, G. New insights into the inhibition of hesperetin on polyphenol oxidase: Inhibitory kinetics, binding characteristics, conformational change and computational simulation. Foods, 2023, 12(4), 905. doi: 10.3390/foods12040905 PMID: 36832979</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Finan, B.; Parlee, S.D.; Yang, B. Nuclear hormone and peptide hormone therapeutics for NAFLD and NASH. Mol. Metab., 2021, 46, 101153. doi: 10.1016/j.molmet.2020.101153 PMID: 33359400</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Mullur, R.; Liu, Y.Y.; Brent, G.A. Thyroid hormone regulation of metabolism. Physiol. Rev., 2014, 94(2), 355-382. doi: 10.1152/physrev.00030.2013 PMID: 24692351</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Ruffolo, R.R., Jr. The pharmacology of dobutamine. Am. J. Med. Sci., 1987, 294(4), 244-248. doi: 10.1097/00000441-198710000-00005 PMID: 3310640</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Ellman, G.L.; Courtney, K.D.; Andres, V., Jr.; Featherstone, R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol., 1961, 7(2), 88-95. doi: 10.1016/0006-2952(61)90145-9 PMID: 13726518</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Yiğit, M.; Celepci, D.B.; Taslimi, P.; Yiğit, B.; Çetinkaya, E.; Özdemir, İ.; Aygün, M.; Gülçin, İ. Selenourea and thiourea derivatives of chiral and achiral enetetramines: Synthesis, characterization and enzyme inhibitory properties. Bioorg. Chem., 2022, 120, 105566. doi: 10.1016/j.bioorg.2021.105566 PMID: 34974209</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Sujayev, A.; Taslimi, P.; Kaya, R.; Safarov, B.; Aliyeva, L.; Farzaliyev, V.; Gulçin, İ. Synthesis, characterization and biological evaluation of N ‐substituted triazinane‐2‐thiones and theoreticalexperimental mechanism of condensation reaction. Appl. Organomet. Chem., 2020, 34(2), e5329. doi: 10.1002/aoc.5329</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Zengin, M.; Genc, H.; Taslimi, P.; Kestane, A.; Guclu, E.; Ogutlu, A.; Karabay, O.; Gulçin, İ. Novel thymol bearing oxypropanolamine derivatives as potent some metabolic enzyme inhibitors  Their antidiabetic, anticholinergic and antibacterial potentials. Bioorg. Chem., 2018, 81, 119-126. doi: 10.1016/j.bioorg.2018.08.003 PMID: 30118983</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Yılmaz, M.A.; Taslimi, P.; Kılıç, Ö.; Gülçin, İ.; Dey, A.; Bursal, E. Unravelling the phenolic compound reserves, antioxidant and enzyme inhibitory activities of an endemic plant species, Achillea pseudoaleppica. J. Biomol. Struct. Dyn., 2023, 41(2), 445-456. doi: 10.1080/07391102.2021.2007792 PMID: 34822320</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Akıncıoğlu, A.; Göksu, S.; Naderi, A.; Akıncıoğlu, H.; Kılınç, N.; Gülçin, İ. Cholinesterases, carbonic anhydrase inhibitory properties and in silico studies of novel substituted benzylamines derived from dihydrochalcones. Comput. Biol. Chem., 2021, 94, 107565. doi: 10.1016/j.compbiolchem.2021.107565 PMID: 34474201</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Tao, Y.; Zhang, Y.; Cheng, Y.; Wang, Y. Rapid screening and identification of α-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR. Biomed. Chromatogr., 2013, 27(2), 148-155. doi: 10.1002/bmc.2761 PMID: 22674728</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Burmaoglu, S.; Yilmaz, A.O.; Taslimi, P.; Algul, O.; Kilic, D.; Gulcin, I. Synthesis and biological evaluation of phloroglucinol derivatives possessing α-glycosidase, acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase inhibitory activity. Arch. Pharm., 2018, 351(2), 1700314. doi: 10.1002/ardp.201700314 PMID: 29323749</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Taslimi, P.; Kandemir, F.M.; Demir, Y.; İleritürk, M.; Temel, Y.; Caglayan, C.; Gulçin, İ. The antidiabetic and anticholinergic effects of chrysin on cyclophosphamide‐induced multiple organ toxicity in rats: Pharmacological evaluation of some metabolic enzyme activities. J. Biochem. Mol. Toxicol., 2019, 33(6), e22313. doi: 10.1002/jbt.22313 PMID: 30801880</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Kuzu, M.; Aslan, A.; Ahmed, I.; Comakli, V.; Demirdag, R.; Uzun, N. Purification of glucose-6-phosphate dehydrogenase and glutathione reductase enzymes from the gill tissue of Lake Van fish and analyzing the effects of some chalcone derivatives on enzyme activities. Fish Physiol. Biochem., 2016, 42(2), 483-491. doi: 10.1007/s10695-015-0153-7 PMID: 26676512</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Türkoğlu, E.A.; Kuzu, M.; Ayasan, T.; Inci, H.; Eratak, S.V. Inhibitory effects of some flavonoids on thioredoxin reductase purified from chicken liver. Braz. J. Poult. Sci., 2019, 21(2), eRBCA-2019-0982. doi: 10.1590/1806-9061-2018-0982</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Temel, Y.; Koçyigit, U.M.; Taysı, M.Ş.; Gökalp, F.; Gürdere, M.B.; Budak, Y.; Ceylan, M.; Gülçin, İ.; Çiftci, M. Purification of glutathione S-transferase enzyme from quail liver tissue and inhibition effects of (3a R, 4 S, 7 R, 7a S)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1 H -4,7-methanoisoindole-1,3(2 H)-dione derivatives on the enzyme activity. J. Biochem. Mol. Toxicol., 2018, 32(3), e22034. doi: 10.1002/jbt.22034 PMID: 29350485</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Metzler, M.; Fischer, L.J. The metabolism of diethylstilbestro. Crit. Rev. Biochem., 1981, 10(3), 171-212. doi: 10.3109/10409238109113599</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Elhennawy, M.G.; Abdelaleem, E.A.; Zaki, A.A.; Mohamed, W.R. Cinnamaldehyde and hesperetin attenuate TNBS‐induced ulcerative colitis in rats through modulation of the JAk2/STAT3/SOCS3 pathway. J. Biochem. Mol. Toxicol., 2021, 35(5), e22730. doi: 10.1002/jbt.22730 PMID: 33522063</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Ren, H.; Hao, J.; Liu, T.; Zhang, D.; Lv, H.; Song, E.; Zhu, C. Hesperetin suppresses inflammatory responses in lipopolysaccharide-induced RAW 264.7 Cells via the Inhibition of NF-κB and activation of Nrf2/HO-1 pathways. Inflammation, 2016, 39(3), 964-973. doi: 10.1007/s10753-016-0311-9 PMID: 26994999</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Cho, J. Antioxidant and neuroprotective effects of hesperidin and its aglycone hesperetin. Arch. Pharm. Res., 2006, 29(8), 699-706. doi: 10.1007/BF02968255 PMID: 16964766</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Svanfelt, J.; Eriksson, J.; Kronberg, L. Analysis of thyroid hormones in raw and treated waste water. J. Chromatogr. A, 2010, 1217(42), 6469-6474. doi: 10.1016/j.chroma.2010.08.032 PMID: 20850122</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Noda, M. Thyroid hormone in the CNS: Contribution of neuronglia interaction. Vitam. Horm., 2018, 106, 313-331. doi: 10.1016/bs.vh.2017.05.005 PMID: 29407440</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Mielgo, V.; Valls i Soler, A.; Rey-Santano, C. Dobutamine in paediatric population: A systematic review in juvenile animal models. PLoS One, 2014, 9(4), e95644. doi: 10.1371/journal.pone.0095644 PMID: 24755688</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Hu, Q.; Guan, X.Q.; Song, L.L.; Wang, H.N.; Xiong, Y.; Liu, J.L.; Yin, H.; Cao, Y.F.; Hou, J.; Yang, L.; Ge, G.B. Inhibition of pancreatic lipase by environmental xenoestrogens. Ecotoxicol. Environ. Saf., 2020, 192, 110305. doi: 10.1016/j.ecoenv.2020.110305 PMID: 32070782</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Maitreesophone, P.; Khine, H.E.E.; Nealiga, J.Q.L.; Kongkatitham, V.; Panuthai, P.; Chaotham, C.; Likhitwitayawuid, K.; Sritularak, B. α-Glucosidase and pancreatic lipase inhibitory effects and anti-adipogenic activity of dendrofalconerol B, a bisbibenzyl from Dendrobium harveyanum. S. Afr. J. Bot., 2022, 146, 187-195. doi: 10.1016/j.sajb.2021.10.025</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Türk, E.; Ozan Tekeli, I.; Özkan, H.; Uyar, A.; Cellat, M.; Kuzu, M.; Yavas, I.; Alizadeh Yegani, A.; Yaman, T.; Güvenç, M. The protective effect of esculetin against aluminium chloride-induced reproductive toxicity in rats. Andrologia, 2021, 53(2), e13930. doi: 10.1111/and.13930 PMID: 33368464</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Taskin, T.; Kahvecioglu, D.; Turkoglu, A.; Dogan, A.; Kuzu, M.; Turkoğlu, A. In vitro biological activities of different extracts from alcea dissecta. Clin. Exp. Heal. Sci., 2022, 12(1), 53-60.</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Gishen, N.Z.; Taddese, S.; Zenebe, T.; Dires, K.; Tedla, A.; Mengiste, B.; Shenkute, D.; Tesema, A.; Shiferaw, Y.; Lulekal, E. In vitro antimicrobial activity of six Ethiopian medicinal plants against Staphylococcus aureus, Escherichia coli and Candida albicans. Eur. J. Integr. Med., 2020, 36, 101121. doi: 10.1016/j.eujim.2020.101121</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Amin Huseen, N.H. Docking Study of naringin binding with COVID-19 main protease enzyme. Iraqi J. Pharm Sci., 2020, 29(2), 231-238. doi: 10.31351/vol29iss2pp231-238</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Rasouli, H.; Hosseini-Ghazvini, S.M.B.; Adibi, H.; Khodarahmi, R. Differential α-amylase/α-glucosidase inhibitory activities of plant-derived phenolic compounds: A virtual screening perspective for the treatment of obesity and diabetes. Food Funct., 2017, 8(5), 1942-1954. doi: 10.1039/C7FO00220C PMID: 28470323</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Kuzu, M.; Kandemir, F.M.; Yıldırım, S.; Çağlayan, C.; Küçükler, S. Attenuation of sodium arsenite-induced cardiotoxicity and neurotoxicity with the antioxidant, anti-inflammatory, and antiapoptotic effects of hesperidin. Environ. Sci. Pollut. Res. Int., 2021, 28(9), 10818-10831. doi: 10.1007/s11356-020-11327-5 PMID: 33099738</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Turk, E.; Kandemir, F.M.; Yildirim, S.; Caglayan, C.; Kucukler, S.; Kuzu, M. Protective effect of hesperidin on sodium arsenite-induced nephrotoxicity and hepatotoxicity in rats. Biol. Trace Elem. Res., 2019, 189(1), 95-108. doi: 10.1007/s12011-018-1443-6 PMID: 30066062</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Li, B.; Huang, A.L.; Zhang, Y.L.; Li, Z.; Ding, H.W.; Huang, C.; Meng, X.M.; Li, J. Design, synthesis and evaluation of hesperetin derivatives as potential multifunctional anti-alzheimer agents. Molecules, 2017, 22(7), 1067. doi: 10.3390/molecules22071067 PMID: 28672874</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Chen, D.W.; Du, Z.; Zhang, C.Z.; Zhang, W.H.; Cao, Y.F.; Sun, H.Z.; Zhu, Z.T.; Yang, K.; Liu, Y.Z.; Zhao, Z.W.; Fu, Z.W.; Gu, W.Q.; Yu, Y.; Fang, Z.Z. The inhibition of UDP-glucuronosyltransferases (UGTs) by tetraiodothyronine (T4) and triiodothyronine (T3). Xenobiotica, 2018, 48(3), 250-257. doi: 10.1080/00498254.2017.1304593 PMID: 28285550</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Fu, A.L.; Zhou, C.Y.; Chen, X. Thyroid hormone prevents cognitive deficit in a mouse model of Alzheimers disease. Neuropharmacology, 2010, 58(4-5), 722-729. doi: 10.1016/j.neuropharm.2009.12.020 PMID: 20045708</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Kizilbay, G.; Karaman, M. Possible inhibition mechanism of dobutamine hydrochloride as potent inhibitor for human glucose-6-phosphate dehydrogenase enzyme. J. Biomol. Struct. Dyn., 2022, 40(1), 204-212. doi: 10.1080/07391102.2020.1811155 PMID: 32835622</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Hassan, M.; Raza, H.; Abbasi, M.A.; Moustafa, A.A.; Seo, S.Y. The exploration of novel Alzheimers therapeutic agents from the pool of FDA approved medicines using drug repositioning, enzyme inhibition and kinetic mechanism approaches. Biomed. Pharmacother., 2019, 109, 2513-2526. doi: 10.1016/j.biopha.2018.11.115 PMID: 30551512</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Ashrafian, H.; Zadeh, E.H.; Khan, R.H. Review on Alzheimers disease: Inhibition of amyloid beta and tau tangle formation. Int. J. Biol. Macromol., 2021, 167, 382-394. doi: 10.1016/j.ijbiomac.2020.11.192 PMID: 33278431</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Popescu, I.; Yin, G.; Velmurugan, S.; Erickson, J.R.; Despa, F.; Despa, S. Lower sarcoplasmic reticulum Ca2+ threshold for triggering afterdepolarizations in diabetic rat hearts. Heart Rhythm, 2019, 16(5), 765-772. doi: 10.1016/j.hrthm.2018.11.001 PMID: 30414461</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Sugimoto, H.; Ogura, H.; Arai, Y.; Iimura, Y.; Yamanishi, Y. Research and development of donepezil hydrochloride, a new type of acetylcholinesterase inhibitor. Jpn. J. Pharmacol., 2002, 89(1), 7-20. doi: 10.1254/jjp.89.7 PMID: 12083745</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Syaifie, P.H.; Widya Hemasita, A.; Nugroho, D.W.; Mardliyati, E.; Anshori, I. In Silico investigation of propolis compounds as potential neuroprotective agent. Biointerface Res. Appl. Chem., 2021, 12(6), 8285-8306. doi: 10.33263/BRIAC126.82858306</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Vitorović-Todorović, M.; Cvijetić, I.; Zloh, M.; Perdih, A. Molecular recognition of acetylcholinesterase and its subnanomolar reversible inhibitor: A molecular simulations study. J. Biomol. Struct. Dyn., 2022, 40(4), 1671-1691. doi: 10.1080/07391102.2020.1831960 PMID: 33047663</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Aleixandre, A.; Gil, J.V.; Sineiro, J.; Rosell, C.M. Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions. Food Chem., 2022, 372, 131231. doi: 10.1016/j.foodchem.2021.131231 PMID: 34624776</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Li, Y.; Sang, S.; Ren, W.; Pei, Y.; Bian, Y.; Chen, Y.; Sun, H. Inhibition of Histone Deacetylase 6 (HDAC6) as a therapeutic strategy for Alzheimers disease: A review (2010-2020). Eur. J. Med. Chem., 2021, 226, 113874. doi: 10.1016/j.ejmech.2021.113874 PMID: 34619465</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Padhi, S.; Dash, M.; Behera, A. Nanophytochemicals for the treatment of type II diabetes mellitus: A review. Environ. Chem. Lett., 2021, 19(6), 4349-4373. doi: 10.1007/s10311-021-01283-y</mixed-citation></ref></ref-list></back></article>
