Bifunctional phenolic-choline conjugates as anti-oxidants and acetylcholinesterase inhibitors

References

• Casetta I, Govoni V, Granieri E. Oxidative stress, antioxidants and neurodegenerative diseases. Curr Pharm Des 2005;11:2033–2052.
   PubMed Web of Science ®Google Scholar
• Lau I-F Brodney, MA. Therapeutic approaches for the treatment of Alzheimer disease: an Overview. In: Lau I-F Brodney, MA (eds), Alzheimer’s Disease. Berlin: Springer-Verlag, 2008, pp. 1–25.
   Google Scholar
• Jakob-Roetne R, Jacobsen H. Alzheimer’s disease: from pathology to therapeutic approaches. Angew Chem Int Ed Engl 2009;48:3030–3059.
   PubMed Web of Science ®Google Scholar
• Mimica N, Presecki P. Current treatment options for people with Alzheimer’s disease in Croatia. Chem Biol Interact 2010;187:409–410.
   PubMed Web of Science ®Google Scholar
• Tumiatti V, Bolognesi ML, Minarini A, Rosini M, Milelli A, Matera R, Melchiorre C. Progress in acetylcholinesterase inhibitors for Alzheimer’s disease: an update. Expert Opin Ther Patents 2008;18:387–401.
   Web of Science ®Google Scholar
• Kao J, Grossberg G. Cholinesterase inhibitors. In: Lau I-F Brodney, MA (eds), Alzheimer’s Disease. Berlin: Springer-Verlag, 2008, pp. 26–51.
   Google Scholar
• Cornelli U. Treatment of Alzheimer’s disease with a cholinesterase inhibitor combined with antioxidants. Neurodegener Dis 2010;7:193–202.
   PubMed Web of Science ®Google Scholar
• Mattson MP. Pathways towards and away from Alzheimer’s disease. Nature 2004;430:631–639.
   PubMed Web of Science ®Google Scholar
• Sayre LM, Perry G, Smith MA. Oxidative stress and neurotoxicity. Chem Res Toxicol 2008;21:172–188.
   PubMed Web of Science ®Google Scholar
• Gaeta A, Hider RC. The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy. Br J Pharmacol 2005;146:1041–1059.
   PubMed Web of Science ®Google Scholar
• Biran Y, Masters CL, Barnham KJ, Bush AI, Adlard PA. Pharmacotherapeutic targets in Alzheimer’s disease. J Cell Mol Med 2009;13:61–86.
   PubMed Web of Science ®Google Scholar
• Rosini M, Andrisano V, Bartolini M, Bolognesi ML, Hrelia P, Minarini A et al. Rational approach to discover multipotent anti-Alzheimer drugs. J Med Chem 2005;48:360–363.
   PubMed Web of Science ®Google Scholar
• Bolognesi ML, Cavalli A, Valgimigli L, Bartolini M, Rosini M, Andrisano V et al. Multi-target-directed drug design strategy: from a dual binding site acetylcholinesterase inhibitor to a trifunctional compound against Alzheimer’s disease. J Med Chem 2007;50:6446–6449.
   PubMed Web of Science ®Google Scholar
• Bolognesi ML, Matera R, Minarini A, Rosini M, Melchiorre C. Alzheimer’s disease: new approaches to drug discovery. Curr Opin Chem Biol 2009;13:303–308.
   PubMed Web of Science ®Google Scholar
• Zheng H, Youdim MB, Fridkin M. Site-activated multifunctional chelator with acetylcholinesterase and neuroprotective-neurorestorative moieties for Alzheimer’s therapy. J Med Chem 2009;52:4095–4098.
   PubMed Web of Science ®Google Scholar
• Arduino D, Silva D, Cardoso SM, Chaves S, Oliveira CR, Santos MA. New hydroxypyridinone iron-chelators as potential anti-neurodegenerative drugs. Front Biosci 2008;13:6763–6774.
   PubMed Web of Science ®Google Scholar
• Koufaki M, Theodorou E, Galaris D, Nousis L, Katsanou ES, Alexis MN. Chroman/catechol hybrids: synthesis and evaluation of their activity against oxidative stress induced cellular damage. J Med Chem 2006;49:300–306.
   PubMed Web of Science ®Google Scholar
• Sanbongi C, Takano H, Osakabe N, Sasa N, Natsume M, Yanagisawa R et al. Rosmarinic acid inhibits lung injury induced by diesel exhaust particles. Free Radic Biol Med 2003;34:1060–1069.
   PubMed Web of Science ®Google Scholar
• Yang JQ, Zhou QX, Liu BZ, He BC. Protection of mouse brain from aluminum-induced damage by caffeic acid. CNS Neurosci Ther 2008;14:10–16.
   PubMed Web of Science ®Google Scholar
• Snape MF, Misra A, Murray TK, De Souza RJ, Williams JL, Cross AJ et al. A comparative study in rats of the in vitro and in vivo pharmacology of the acetylcholinesterase inhibitors tacrine, donepezil and NXX-066. Neuropharmacology 1999;38:181–193.
   PubMed Web of Science ®Google Scholar
• Alemany A, Baluja G, Corral C, Leon JLF. Inhibidores de colinesterasa. 1. Influencia de la estructura del grupo acilo en la inhibicion de colinesterasa por esteres de colina. Anales Real Soc Espan Fis Quim 1962;B58:531–538.
   Google Scholar
• Grigoryan HA, Hambardzumyan AA, Mkrtchyan MV, Topuzyan VO, Halebyan GP, Asatryan RS. alpha,beta-Dehydrophenylalanine choline esters, a new class of reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. Chem Biol Interact 2008;171:108–116.
   PubMed Web of Science ®Google Scholar
• Armarego WLF, Perrin DD. Purification of Laboratory Chemicals, 4th edn. Oxford: Butterworth-Heinemann, 1996.
   Google Scholar
• Ingkaninan K, Temkitthawon P, Chuenchom K, Yuyaem T, Thongnoi W. Screening for acetylcholinesterase inhibitory activity in plants used in Thai traditional rejuvenating and neurotonic remedies. J Ethnopharmacol 2003;89:261–264.
   PubMed Web of Science ®Google Scholar
• Jung YH, Kim JD. Mechanism studies on the CSI reaction with allyl ethers by varying p-substituent. Arch Pharm Res 2003;26:667–678.
   PubMed Web of Science ®Google Scholar
• Bisogno F, Mascoti L, Sanchez C, Garibotto F, Giannini F, Kurina-Sanz M et al. Structure-antifungal activity relationship of cinnamic acid derivatives. J Agric Food Chem 2007;55:10635–10640.
   PubMed Web of Science ®Google Scholar
• Tepe B, Daferera D, Sokmen A, Sokmen M, Polissiou M. Antimicrobial and antioxidant activities of the essential oil and various extracts of Salvia tomentosa Miller (Lamiaceae). Food Chem 2005;90:333–340.
   Web of Science ®Google Scholar
• Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H et al. The Protein Data Bank. Nucleic Acids Res 2000;28:235–242.
   PubMed Web of Science ®Google Scholar
• Maestro, version 7.5; Schrödinger Inc.: Portland, OR, 2005.
   Google Scholar
• Macromodel, version 8.5; Schrödinger Inc.: Portland, OR, 1999.
   Google Scholar
• Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267:727–748.
   PubMed Web of Science ®Google Scholar
• QikProp, version 2.5, Schrödinger, LLC, New York, NY, 2005.
   Google Scholar
• Di L, Kerns EH, Carter GT. Strategies to assess blood–brain barrier penetration. Expert Opin Drug Discov 2008;3:677–687.
   PubMed Web of Science ®Google Scholar
• Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 1983;65:55–63.
   PubMed Web of Science ®Google Scholar
• López S, Bastida J, Viladomat F, Codina C. Acetylcholinesterase inhibitory activity of some Amaryllidaceae alkaloids and Narcissus extracts. Life Sci 2002;71:2521–2529.
   PubMed Web of Science ®Google Scholar
• Giacobini E. Drugs that target cholinesterase. In: Buccafusco J (ed), Cognitive Enhancing Drugs. Switzerland: Birkhauser Verlag, 2004, pp. 11–37.
   Google Scholar
• Bolognesi ML, Bartolini M, Cavalli A, Andrisano V, Rosini M, Minarini A et al. Design, synthesis, and biological evaluation of conformationally restricted rivastigmine analogues. J Med Chem 2004;47:5945–5952.
   PubMed Web of Science ®Google Scholar
• Wlodek ST, Antosiewicz J, Briggs JM. On the Mechanism of acetylcholinesterase action: the electrostatically induced acceleration of the catalytic acylation step. J Am Chem Soc 1997;119:8159–8165.
   Web of Science ®Google Scholar
• Tõugu V. Acetylcholinesterase: mechanism of catalysis and inhibition. Curr Med Chem CNS Agents 2001;1:155–170.
   Google Scholar
• Colletier J-P Fournier, D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M. Structural insights into substrate traffic and inhibition in acetylcholinesterase. EMBO J 2006;25:2746–2756.
   PubMed Web of Science ®Google Scholar
• Kryger G, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs. Structure 1999;7:297–307.
   PubMed Web of Science ®Google Scholar
• Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C et al. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Natl Acad Sci USA 1993;90:9031–9035.
   PubMed Web of Science ®Google Scholar
• Valko M, Rhodes CJ, Moncol J, Izakovic M, Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact 2006;160:1–40.
   PubMed Web of Science ®Google Scholar
• Denisov ET, Afanas’ev IB. Oxidation and Antioxidants in Organic Chemistry and Biology. Boca Raton, FL: CRC Press, 2005:835–894.
   Google Scholar
• Youdim MB, Amit T, Bar-Am O, Weinstock M, Yogev-Falach M. Amyloid processing and signal transduction properties of antiparkinson-antialzheimer neuroprotective drugs rasagiline and TV3326. Ann N Y Acad Sci 2003;993:378–86; discussion 387.
   PubMed Web of Science ®Google Scholar
• Cardoso SM, Moreira PI, Agostinho P, Pereira C, Oliveira CR. Neurodegenerative pathways in Parkinson’s disease: therapeutic strategies. Curr Drug Targets CNS Neurol Disord 2005;4:405–419.
   PubMedGoogle Scholar
• Pereira C, Agostinho P, Moreira PI, Cardoso SM, Oliveira CR. Alzheimer’s disease-associated neurotoxic mechanisms and neuroprotective strategies. Curr Drug Targets CNS Neurol Disord 2005;4:383–403.
   PubMedGoogle Scholar
• Esteves AR, Domingues AF, Ferreira IL, Januário C, Swerdlow RH, Oliveira CR et al. Mitochondrial function in Parkinson’s disease cybrids containing an nt2 neuron-like nuclear background. Mitochondrion 2008;8:219–228.
   PubMed Web of Science ®Google Scholar
• Cardoso SM, Santos S, Swerdlow RH, Oliveira CR. Functional mitochondria are required for amyloid beta-mediated neurotoxicity. Faseb J 2001;15:1439–1441.
   PubMed Web of Science ®Google Scholar
• Troy CM, Shelanski ML. Caspase-2 redux. Cell Death Differ 2003;10:101–107.
   PubMed Web of Science ®Google Scholar
• Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, Koyama Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004;165:347–356.
   PubMed Web of Science ®Google Scholar
• Otoguro K, Kuno F, Omura S. Arisugacins, selective acetylcholinesterase inhibitors of microbial origin. Pharmacol Ther 1997;76:45–54.
   PubMed Web of Science ®Google Scholar
• Mata T, Proença C, Ferreira AR, Serralheiro MLM, Nogueira JMF, Araújo MEM. Antioxidant and antiacetylcholinesterase activities of five plants used as Portuguese food spices. Food Chem 2007;103:778–786.
   Web of Science ®Google Scholar