Design, synthesis and evaluation of new chromone-derived aminophosphonates as potential acetylcholinesterase inhibitor.
Acetylcholinesterase
/ chemistry
Antioxidants
/ chemical synthesis
Biphenyl Compounds
/ chemistry
Butyrylcholinesterase
/ chemistry
Cholinesterase Inhibitors
/ chemical synthesis
Chromones
/ chemical synthesis
DNA
/ chemistry
Drug Design
Hydrogen Peroxide
/ chemistry
Lipase
/ chemistry
Molecular Docking Simulation
Organophosphonates
/ chemical synthesis
Picrates
/ chemistry
Acetylcholinesterase inhibitors
Antioxidant studies
Catalysis
DNA cleavage
Molecular docking
Journal
Molecular diversity
ISSN: 1573-501X
Titre abrégé: Mol Divers
Pays: Netherlands
ID NLM: 9516534
Informations de publication
Date de publication:
May 2021
May 2021
Historique:
received:
22
11
2019
accepted:
21
02
2020
pubmed:
4
3
2020
medline:
23
11
2021
entrez:
4
3
2020
Statut:
ppublish
Résumé
A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE ranged between 0.103 and 5.781 µM, whereas for BuChE, activities ranged between 8.619 and 18.789 µM. The results show that among the various synthesized compounds, strongest AChE inhibition was found for the compound containing aliphatic amine analogs, while in case of BuChE, aromatic amines showed better activity as compared to aliphatic amines. Compound 4j was found to be the most potent inhibitor of AChE with an IC
Identifiants
pubmed: 32124162
doi: 10.1007/s11030-020-10060-y
pii: 10.1007/s11030-020-10060-y
doi:
Substances chimiques
Antioxidants
0
Biphenyl Compounds
0
Cholinesterase Inhibitors
0
Chromones
0
Organophosphonates
0
Picrates
0
DNA
9007-49-2
Hydrogen Peroxide
BBX060AN9V
1,1-diphenyl-2-picrylhydrazyl
DFD3H4VGDH
Lipase
EC 3.1.1.3
Acetylcholinesterase
EC 3.1.1.7
Butyrylcholinesterase
EC 3.1.1.8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
811-825Références
Shrivastava SK, Sinha SK, Srivastava P, Tripathi PN, Sharma P, Tripathi MK, Tripathi A, Choubey PK, Waiker DK, Aggarwal LM, Dixit M, Kheruka SC, Gambhir S, Shankar S, Srivastava RK (2019) Design and development of novel p-aminobenzoic acid derivatives as potential cholinesterase inhibitors for the treatment of Alzheimer’s disease. Bioorgan Chem 82:211–223. https://doi.org/10.1016/j.bioorg.2018.10.009
doi: 10.1016/j.bioorg.2018.10.009
Kung HF, Lee CW, Zhuang ZP, Kung MP, Hou C, Plössl K (2001) Novel stilbenes as probes for amyloid plaques. J Am Chem Soc 123:12740–12741. https://doi.org/10.1021/ja0167147
doi: 10.1021/ja0167147
pubmed: 11741464
Viau CJ, Curren RO, Wallace K (1993) Cytotoxicity of tacrine and velnacrine metabolites in cultured rat, dog and human hepatocytes. Drug Chem Toxicol 16:227–239. https://doi.org/10.3109/01480549309081817
doi: 10.3109/01480549309081817
pubmed: 8404544
Gaspar A, Matos MJ, Garrido J, Uriarte E, Borges F (2014) Chromone: a valid scaffold in medicinal chemistry. Chem Rev 114:4960–4992. https://doi.org/10.1021/cr400265z
doi: 10.1021/cr400265z
pubmed: 24555663
Agullo G, Gamet-Payrastre L, Manenti S, Viala C, Rémésy C, Chap H, Payrastre B (1997) Relationship between flavonoid structure and inhibition of phosphatidylinositol 3-kinase: a comparison with tyrosine kinase and protein kinase C inhibition. Biochem Pharmacol 53:1649–1657. https://doi.org/10.1016/S0006-2952(97)82453-7
doi: 10.1016/S0006-2952(97)82453-7
pubmed: 9264317
Khan KM, Ambreen N, Mughal UR, Jalil S, Perveen S, Choudhary MI (2010) 3-Formylchromones: potential antiinflammatory agents. Eur J Med Chem 45:4058–4064. https://doi.org/10.1016/j.ejmech.2010.05.065
doi: 10.1016/j.ejmech.2010.05.065
pubmed: 20576329
Jackson SP, Schoenwaelder SM (2003) Antiplatelet therapy: in search of the “magic bullet”. Nat Rev Drug Discov 2:775–789. https://doi.org/10.1038/nrd1198
doi: 10.1038/nrd1198
pubmed: 14526381
Khan KM, Ahmad A, Ambreen N, Amyn A, Perveen S, Khan SA, Choudhary MI (2009) Schiff bases of 3- formylchromones as antibacterial, antifungal, and phytotoxic agents. Lett Drug Des Discov 6:363–373
doi: 10.2174/1570180810906050363
Miean KH, Mohamed S (2001) Flavonoid (myricetin, quercetin, kaempferol, luteolin, and apigenin) content of edible tropical plants. J Agric Food Chem 49:3106–3112. https://doi.org/10.1021/jf000892m
doi: 10.1021/jf000892m
pubmed: 11410016
Viayna E, Sabate R, Muñoz-Torrero D (2014) Dual inhibitors of β-amyloid aggregation and acetylcholinesterase as multi-target anti-Alzheimer drug candidates. Curr Top Med Chem 13:1820–1842. https://doi.org/10.2174/15680266113139990139
doi: 10.2174/15680266113139990139
Brühlmann C, Ooms F, Carrupt PA, Testa B, Catto M, Leonetti F, Altomare C, Carotti A (2001) Coumarins derivatives as dual inhibitors of acetylcholinesterase and monoamine oxidase. J Med Chem 44:3195–3198. https://doi.org/10.1021/jm010894d
doi: 10.1021/jm010894d
pubmed: 11543689
Demmer CS, Krogsgaard-Larsen N, Bunch L (2011) Review on modern advances of chemical methods for the introduction of a phosphonic acid group. Chem Rev 111:7981–8006. https://doi.org/10.1021/cr2002646
doi: 10.1021/cr2002646
pubmed: 22010799
Sienczyk M, Oleksyszyn J (2009) Irreversible inhibition of serine proteases—design and in vivo activity of diaryl β-aminophosphonate derivatives. Curr Med Chem 16:1673–1687. https://doi.org/10.2174/092986709788186246
doi: 10.2174/092986709788186246
pubmed: 19442139
Atherton FR, Hassall CH, Lambert RW (1986) Synthesis and structure-activity relationships of antibacterial phosphonopeptides incorporating (1-aminoethyl)phosphonic acid and (aminomethyl)phosphonic acid. J Med Chem 29:29–40. https://doi.org/10.1021/jm00151a005
doi: 10.1021/jm00151a005
pubmed: 3510298
Thaslim Basha S, Sudhamani H, Rasheed S, Venkateswarlu N, Vijaya T, Naga Raju C (2016) Microwave-assisted neat synthesis of α-aminophosphonate/phosphinate derivatives of 2-(2-aminophenyl)benzothiazole as potent antimicrobial and antioxidant agents. Phosphorus Sulfur Silicon Relat Elem 191:1339–1343. https://doi.org/10.1080/10426507.2016.1192629
doi: 10.1080/10426507.2016.1192629
Bhagat S, Shah P, Garg SK, Mishra S, Kamal Kaur P, Singh S, Chakraborti AK (2014) Aminophosphonates as novel anti-leishmanial chemotypes: synthesis, biological evaluation, and CoMFA studies. Medchemcomm 5:665–670. https://doi.org/10.1039/c3md00388d
doi: 10.1039/c3md00388d
Valasani KR, Hu G, Chaney MO, Yan SS (2013) Structure-based design and synthesis of benzothiazole phosphonate analogues with inhibitors of human ABAD-Aβ for treatment of Alzheimer’s disease. Chem Biol Drug Des 81:238–249. https://doi.org/10.1111/cbdd.12068
doi: 10.1111/cbdd.12068
pubmed: 23039767
Luo W, Bin SuY, Hong C, Tian RG, Su LP, Wang YQ, Li Y, Yue JJ, Wang CJ (2013) Design, synthesis and evaluation of novel 4-dimethylamine flavonoid derivatives as potential multi-functional anti-Alzheimer agents. Bioorgan Med Chem 21:7275–7282. https://doi.org/10.1016/j.bmc.2013.09.061
doi: 10.1016/j.bmc.2013.09.061
Luo W, Chen Y, Wang T, Hong C, Chang LP, Chang CC, Yang YC, Xie SQ, Wang CJ (2016) Design, synthesis and evaluation of novel 7-aminoalkyl-substituted flavonoid derivatives with improved cholinesterase inhibitory activities. Bioorgan Med Chem 24:672–680. https://doi.org/10.1016/j.bmc.2015.12.031
doi: 10.1016/j.bmc.2015.12.031
Li RS, Wang XB, Hu XJ, Kong LY (2013) Design, synthesis and evaluation of flavonoid derivatives as potential multifunctional acetylcholinesterase inhibitors against Alzheimer’s disease. Bioorgan Med Chem Lett 23:2636–2641. https://doi.org/10.1016/j.bmcl.2013.02.095
doi: 10.1016/j.bmcl.2013.02.095
Fernández-Bachiller MI, Pérez C, Monjas L, Rademann J, Rodríguez-Franco MI (2012) New tacrine-4-oxo-4H-chromene hybrids as multifunctional agents for the treatment of Alzheimer’s disease, with cholinergic, antioxidant, and β-amyloid-reducing properties. J Med Chem 55:1303–1317. https://doi.org/10.1021/jm201460y
doi: 10.1021/jm201460y
pubmed: 22243648
Xu JC, Li WM, Zheng H, Lai YF, Zhang PF (2011) One-pot synthesis of tetrahydrochromene derivatives catalyzed by lipase. Tetrahedron 67:9582–9587. https://doi.org/10.1016/j.tet.2011.09.137
doi: 10.1016/j.tet.2011.09.137
Liang YR, Hu YJ, Zhou XH, Wu Q, Lin XF (2017) One-pot construction of spirooxindole backbone via biocatalytic domino reaction. Tetrahedron Lett 58:2923–2926. https://doi.org/10.1016/j.tetlet.2017.06.031
doi: 10.1016/j.tetlet.2017.06.031
Wiktelius D (2005) Lipases—enzymes for biocatalytic asymmetric synthesis. Synlett. https://doi.org/10.1055/s-2005-872233
doi: 10.1055/s-2005-872233
Wang JL, Liu BK, Yin C, Wu Q, Lin XF (2011) Candida antarctica lipase B-catalyzed the unprecedented three-component Hantzsch-type reaction of aldehyde with acetamide and 1,3-dicarbonyl compounds in non-aqueous solvent. Tetrahedron 67:2689–2692. https://doi.org/10.1016/j.tet.2011.01.045
doi: 10.1016/j.tet.2011.01.045
Hu W, Guan Z, Deng X, He YH (2012) Enzyme catalytic promiscuity: the papain-catalyzed Knoevenagel reaction. Biochimie 94:656–661. https://doi.org/10.1016/j.biochi.2011.09.018
doi: 10.1016/j.biochi.2011.09.018
pubmed: 21963435
Li K, He T, Li C, Feng XW, Wang N, Yu XQ (2009) Lipase-catalysed direct Mannich reaction in water: utilization of biocatalytic promiscuity for C–C bond formation in a “one-pot” synthesis. Green Chem 11:777–779. https://doi.org/10.1039/b817524a
doi: 10.1039/b817524a
Xie ZB, Wang N, Zhou LH, Wan F, He T, Le ZG, Yu XQ (2013) Lipase-catalyzed stereoselective cross-aldol reaction promoted by water. ChemCatChem 5:1935–1940. https://doi.org/10.1002/cctc.201200890
doi: 10.1002/cctc.201200890
Xu KL, Guan Z, He YH (2011) Acidic proteinase from Aspergillus usamii catalyzed Michael addition of ketones to nitroolefins. J Mol Catal B Enzym 71:108–112. https://doi.org/10.1016/j.molcatb.2011.04.005
doi: 10.1016/j.molcatb.2011.04.005
Guezane-Lakoud S, Toffano M, Aribi-Zouioueche L (2017) Promiscuous lipase catalyzed a new P–C bond formation: green and efficient protocol for one-pot synthesis of α-aminophosphonates. Heteroat Chem 28:1–11. https://doi.org/10.1002/hc.21408
doi: 10.1002/hc.21408
Ellman GL, Courtney KD, Andres V, Featherstone RM (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88–95
doi: 10.1016/0006-2952(61)90145-9
Nunomura A, Castellani RJ, Zhu X, Moreira PI, Perry G, Smith MA (2006) Involvement of oxidative stress in Alzheimer disease. J Neuropathol Exp Neurol 65:631–641. https://doi.org/10.1097/01.jnen.0000228136.58062.bf
doi: 10.1097/01.jnen.0000228136.58062.bf
pubmed: 16825950
Guzior N, Wieckowska A, Panek D, Malawska B (2014) Recent development of multifunctional agents as potential drug candidates for the treatment of Alzheimer’s disease. Curr Med Chem 22:373–404. https://doi.org/10.2174/0929867321666141106122628
doi: 10.2174/0929867321666141106122628
Gulcin I, Buyukokuroglu ME, Kufrevioglu OI (2003) Metal chelating and hydrogen peroxide scavenging effects of melatonin. J Pineal Res 34:278–281. https://doi.org/10.1034/j.1600-079X.2003.00042.x
doi: 10.1034/j.1600-079X.2003.00042.x
pubmed: 12662350
Jorge MP, Madjarof C, Ruiz ALTG, Fernandes AT, Rodrigues RAF, de Oliveira Sousa IM, Foglio MA, de Carvalho JE (2008) Evaluation of wound healing properties of Arrabidaea chica Verlot extract. J Ethnopharmacol 118:361–366. https://doi.org/10.1016/j.jep.2008.04.024
doi: 10.1016/j.jep.2008.04.024
pubmed: 18573628
Ames BN (1984) Dietary carcinogens and anti-carcinogens. J Toxicol Clin Toxicol 22:291–301. https://doi.org/10.3109/15563658408992561
doi: 10.3109/15563658408992561
pubmed: 6502792
Kumar V, Lemos M, Sharma M, Shriram V (2013) Antioxidant and DNA damage protecting activities of Eulophia nuda Lindl. Free Radic Antioxid 3:55–60. https://doi.org/10.1016/j.fra.2013.07.001
doi: 10.1016/j.fra.2013.07.001
Salar RK, Purewal SS, Sandhu KS (2017) Relationships between DNA damage protection activity, total phenolic content, condensed tannin content and antioxidant potential among Indian barley cultivars. Biocatal Agric Biotechnol 11:201–206. https://doi.org/10.1016/j.bcab.2017.07.006
doi: 10.1016/j.bcab.2017.07.006
Blois MS (1958) Antioxidant determinations by the use of a stable free radical. Nature 181:1199–1200. https://doi.org/10.1038/1811199a0
doi: 10.1038/1811199a0
Liu J, Sun H, Dong F, Xue Q, Wang G, Qin S, Guo Z (2009) The influence of the cation of quaternized chitosans on antioxidant activity. Carbohydr Polym 78:439–443. https://doi.org/10.1016/j.carbpol.2009.04.030
doi: 10.1016/j.carbpol.2009.04.030
Joshi AJ, Bhojwani HR, Joshi UJ (2018) Strategies to select the best pharmacophore model: a case study in pyrazoloquinazoline class of PLK-1 inhibitors. Med Chem Res 27:234–260. https://doi.org/10.1007/s00044-017-2057-9
doi: 10.1007/s00044-017-2057-9
Joshi AJ, Gadhwal MK, Joshi UJ (2014) A combined approach based on 3D pharmacophore and docking for identification of new aurora A kinase inhibitors. Med Chem Res 23:1414–1436. https://doi.org/10.1007/s00044-013-0747-5
doi: 10.1007/s00044-013-0747-5