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Volumn 11, Issue 4, 2011, Pages 4030-4042

Surface plasmon resonance based biosensors for exploring the influence of alkaloids on aggregation of amyloid-β peptide

Author keywords

Alkaloids; Amyloid Peptide; Surface plasmon resonance; Thioaliphatic acid monolayer

Indexed keywords

ALKALOID; AMYLOID BETA PROTEIN; GOLD;

EID: 79953854349     PISSN: 14248220     EISSN: None     Source Type: Journal    
DOI: 10.3390/s110404030     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E.H.; Lansbury, P.T.; Kelly, J.W. Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. USA 1999, 96, 9989-9990.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 75149136696 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid-beta peptide
    • Murphy, M.P.; LeVine, H., III. Alzheimer's disease and the amyloid-beta peptide. J. Alzheimers Dis. 2010, 19, 311-323.
    • (2010) J. Alzheimers Dis , vol.19 , pp. 311-323
    • Murphy, M.P.1    Levine III, H.2
  • 5
    • 33645513980 scopus 로고    scopus 로고
    • Theoretical approaches to protein aggregation
    • Gsponer, J.; Vendruscolo, M. Theoretical approaches to protein aggregation. Protein Pept. Lett. 2006, 13, 287-293.
    • (2006) Protein Pept. Lett , vol.13 , pp. 287-293
    • Gsponer, J.1    Vendruscolo, M.2
  • 7
    • 32844461888 scopus 로고    scopus 로고
    • Nicotinic effects on cognitive function: Behavioural characterization, pharmacological specification, and anatomic localization
    • (Berlin)
    • Levin, E.D.; McClernon, F.J.; Rezvani, A.H. Nicotinic effects on cognitive function: Behavioural characterization, pharmacological specification, and anatomic localization. Psychopharmacology (Berlin) 2006, 184, 523-539.
    • (2006) Psychopharmacology , vol.184 , pp. 523-539
    • Levin, E.D.1    McClernon, F.J.2    Rezvani, A.H.3
  • 8
    • 0034076985 scopus 로고    scopus 로고
    • Prospects for pharmacological intervention in Alzheimer disease
    • Emilien, G.; Beyreuther, K.; Masters, C.L.; Maloteaux, J.M. Prospects for pharmacological intervention in Alzheimer disease. Arch Neurol. 2000, 57, 454-459.
    • (2000) Arch Neurol , vol.57 , pp. 454-459
    • Emilien, G.1    Beyreuther, K.2    Masters, C.L.3    Maloteaux, J.M.4
  • 9
    • 0035251815 scopus 로고    scopus 로고
    • Nicotine and its interaction with beta-amyloid protein: A short review
    • Zamani, M.R.; Allen, Y.S. Nicotine and its interaction with beta-amyloid protein: A short review. Biol. Psychiatry 2001, 49, 221-232.
    • (2001) Biol. Psychiatry , vol.49 , pp. 221-232
    • Zamani, M.R.1    Allen, Y.S.2
  • 10
    • 34247199857 scopus 로고    scopus 로고
    • Application of nicotine enantiomers, derivatives and analogues in therapy of neurodegenerative disorders
    • Pogocki, D.; Ruman, T.; Danilczuk, M.; Celuch, M.; Wałajtys-Rode, E. Application of nicotine enantiomers, derivatives and analogues in therapy of neurodegenerative disorders. Eur. J. Pharmacol. 2007, 563, 18-39.
    • (2007) Eur. J. Pharmacol , vol.563 , pp. 18-39
    • Pogocki, D.1    Ruman, T.2    Danilczuk, M.3    Celuch, M.4    Wałajtys-Rode, E.5
  • 14
    • 0036838889 scopus 로고    scopus 로고
    • Nicotine breaks down preformed Alzheimer's beta-amyloid fibrils in vitro
    • Ono, K.; Hasegawa, K.; Yamada, M.; Naiki, H. Nicotine breaks down preformed Alzheimer's beta-amyloid fibrils in vitro. Biol. Psychiatry 2002, 52, 880-886.
    • (2002) Biol. Psychiatry , vol.52 , pp. 880-886
    • Ono, K.1    Hasegawa, K.2    Yamada, M.3    Naiki, H.4
  • 15
    • 33847356841 scopus 로고    scopus 로고
    • Electrochemical impedance spectroscopy for study of amyloid beta-peptide interactions with (-) nicotine ditartrate and (-) cotinine
    • Szymańska, I.; Radecka, H.; Radecki, J.; Kaliszan, R. Electrochemical impedance spectroscopy for study of amyloid beta-peptide interactions with (-) nicotine ditartrate and (-) cotinine. Biosens. Bioelectron. 2007, 22, 1955-1960.
    • (2007) Biosens. Bioelectron , vol.22 , pp. 1955-1960
    • Szymańska, I.1    Radecka, H.2    Radecki, J.3    Kaliszan, R.4
  • 16
    • 77949664680 scopus 로고    scopus 로고
    • Association constants of pyridine and piperidine alkaloids to amyloid beta peptide determined by electrochemical impedance spectroscopy
    • Grabowska, I.; Radecka, H.; Burza, A.; Radecki, J.; Kaliszan, M.; Kaliszan, R. Association constants of pyridine and piperidine alkaloids to amyloid beta peptide determined by electrochemical impedance spectroscopy. Curr. Alzheimer Res. 2010, 7, 165-172.
    • (2010) Curr. Alzheimer Res , vol.7 , pp. 165-172
    • Grabowska, I.1    Radecka, H.2    Burza, A.3    Radecki, J.4    Kaliszan, M.5    Kaliszan, R.6
  • 18
    • 15844369794 scopus 로고    scopus 로고
    • Surface plasmon resonance for the analysis of beta-amyloid interactions and fibril formation in Alzheimer's disease research
    • Aguilar, M.I.; Small, D.H. Surface plasmon resonance for the analysis of beta-amyloid interactions and fibril formation in Alzheimer's disease research. Neurotox. Res. 2005, 7, 17-27.
    • (2005) Neurotox. Res , vol.7 , pp. 17-27
    • Aguilar, M.I.1    Small, D.H.2
  • 19
    • 33744510885 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing
    • Hu, W.P.; Chang, G.L.; Chen, S.J.; Kuo, Y.M. Kinetic analysis of beta-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing. J. Neurosci. Meth. 2006, 154, 190-197.
    • (2006) J. Neurosci. Meth , vol.154 , pp. 190-197
    • Hu, W.P.1    Chang, G.L.2    Chen, S.J.3    Kuo, Y.M.4
  • 21
    • 2642578354 scopus 로고    scopus 로고
    • Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity
    • Liu, R.; Yuan, B.; Emadi, S.; Zameer, A.; Schulz, P.; McAllister, C.; Lyubchenko, Y.; Goud, G.; Sierks, M.R. Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity. Biochemistry 2004, 43, 6959-6967.
    • (2004) Biochemistry , vol.43 , pp. 6959-6967
    • Liu, R.1    Yuan, B.2    Emadi, S.3    Zameer, A.4    Schulz, P.5    McAllister, C.6    Lyubchenko, Y.7    Goud, G.8    Sierks, M.R.9
  • 23
    • 33847025338 scopus 로고    scopus 로고
    • The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure
    • Hirohata, M.; Hasegawa, K.; Tsutsumi-Yasuhara, S.; Ohhashi, Y.; Ookoshi, T.; Ono, K.; Yamada, M.; Naiki, H. The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure. Biochemistry 2007, 46, 1888-1899.
    • (2007) Biochemistry , vol.46 , pp. 1888-1899
    • Hirohata, M.1    Hasegawa, K.2    Tsutsumi-Yasuhara, S.3    Ohhashi, Y.4    Ookoshi, T.5    Ono, K.6    Yamada, M.7    Naiki, H.8
  • 24
    • 41849116004 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of Alzheimer's beta-amyloid aggregation on a solid surface: From monomers to fully-grown fibrils
    • Ryu, J.; Joung, H.A.; Kim, M.G.; Park, C.B. Surface plasmon resonance analysis of Alzheimer's beta-amyloid aggregation on a solid surface: from monomers to fully-grown fibrils. Anal Chem. 2008, 80, 2400-2407.
    • (2008) Anal Chem , vol.80 , pp. 2400-2407
    • Ryu, J.1    Joung, H.A.2    Kim, M.G.3    Park, C.B.4
  • 25
    • 16244391144 scopus 로고    scopus 로고
    • Improved method for the preparation of carboxylic acid and amine terminated self-assembled monolayers of alkanethiolates
    • Wang, H.; Chen, S.; Li, L.; Jiang, S. Improved method for the preparation of carboxylic acid and amine terminated self-assembled monolayers of alkanethiolates. Langmuir 2005, 21, 2633-2636.
    • (2005) Langmuir , vol.21 , pp. 2633-2636
    • Wang, H.1    Chen, S.2    Li, L.3    Jiang, S.4
  • 27
    • 18844378631 scopus 로고    scopus 로고
    • Surface-induced aggregation of beta amyloid peptide by ω-substituted alkanethiol monolayers supported on gold
    • McMasters, M.J.; Hammer, R.P.; McCarley, R.L. Surface-induced aggregation of beta amyloid peptide by ω-substituted alkanethiol monolayers supported on gold. Langmuir 2005, 21, 4464-4470.
    • (2005) Langmuir , vol.21 , pp. 4464-4470
    • McMasters, M.J.1    Hammer, R.P.2    McCarley, R.L.3
  • 28
    • 77749309609 scopus 로고    scopus 로고
    • Comparative molecular dynamics study of Aβ adsorption on the self-assembled monolayers
    • Wang, Q.; Zhao, C.; Zhao, J.; Wang, J.; Yang, J.-C.; Yu, X.; Zheng, J. Comparative molecular dynamics study of Aβ adsorption on the self-assembled monolayers. Langmuir 2010, 26, 3308-3316.
    • (2010) Langmuir , vol.26 , pp. 3308-3316
    • Wang, Q.1    Zhao, C.2    Zhao, J.3    Wang, J.4    Yang, J.-C.5    Yu, X.6    Zheng, J.7
  • 30
    • 84885838418 scopus 로고    scopus 로고
    • Chemspider
    • Available Online, accessed on 16 February 2011
    • ChemSpider. Available online: http://nature.chemspider.com (accessed on 16 February 2011).
  • 31
    • 34548147556 scopus 로고    scopus 로고
    • The rule of five revisited: Applying log D in place of log P in drug-likeness filters
    • Bhal, S.K.; Kassam, K.; Peirson, I.G.; Pearl, G.M. The rule of five revisited: Applying log D in place of log P in drug-likeness filters. Mol. Pharm. 2007, 4, 556-560.
    • (2007) Mol. Pharm , vol.4 , pp. 556-560
    • Bhal, S.K.1    Kassam, K.2    Peirson, I.G.3    Pearl, G.M.4
  • 32
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • Ono, K.; Hasegawa, K.; Naiki, H.; Yamada, M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J. Neurosci. Res. 2004, 75, 742-750.
    • (2004) J. Neurosci. Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 33
    • 37349062389 scopus 로고    scopus 로고
    • Visualaization and classification of amyloid β supramolecular assemblies
    • Yagi, H.; Ban, T.; Morigaki, K.; Naiki, H.; Goto, Y. Visualaization and classification of amyloid β supramolecular assemblies. Biochemistry 2007, 46, 15009-15017.
    • (2007) Biochemistry , vol.46 , pp. 15009-15017
    • Yagi, H.1    Ban, T.2    Morigaki, K.3    Naiki, H.4    Goto, Y.5
  • 34
    • 53349167620 scopus 로고    scopus 로고
    • Electrochemical assay of human islet amyloid polypeptide and its aggregation
    • Zhou, N.; Chen, Z.; Zhang, D.; Li, G. Electrochemical assay of human islet amyloid polypeptide and its aggregation. Sensors 2008, 8, 5987-5995.
    • (2008) Sensors , vol.8 , pp. 5987-5995
    • Zhou, N.1    Chen, Z.2    Zhang, D.3    Li, G.4
  • 36
    • 0043066616 scopus 로고    scopus 로고
    • Kinetics of adsorption of Abeta(1-40) to lipid bilayers
    • Kremer, J.J.; Murphy, R.M. Kinetics of adsorption of Abeta(1-40) to lipid bilayers. J. Biochem. Biophys. Meth. 2003, 57, 159-169.
    • (2003) J. Biochem. Biophys. Meth , vol.57 , pp. 159-169
    • Kremer, J.J.1    Murphy, R.M.2
  • 37
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and disscociation using surface plasmon resonanace
    • Hasegawa, K.; Ono, K.; Yamada, M.; Naiki, H. Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and disscociation using surface plasmon resonanace. Biochemistry 2002, 41, 13489-13498.
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 38
    • 70349634195 scopus 로고    scopus 로고
    • Exploiting surface plasmon resonance (SPR) technology for the identification of fibroblast growth factor-2 (FGF2) anatgonists endowed with antiangiogenic activity
    • Rusnati, M.; Bugatti, A.; Mitola, S.; Leali, D.; Bergese, P.; Depero, L.E.; Presta, M. Exploiting surface plasmon resonance (SPR) technology for the identification of fibroblast growth factor-2 (FGF2) anatgonists endowed with antiangiogenic activity. Sensors 2009, 9, 6471-6503.
    • (2009) Sensors , vol.9 , pp. 6471-6503
    • Rusnati, M.1    Bugatti, A.2    Mitola, S.3    Leali, D.4    Bergese, P.5    Depero, L.E.6    Presta, M.7
  • 39
    • 79952080736 scopus 로고    scopus 로고
    • Overview of the characteristic of micro- and nanao-structured surface plasmon resonanace
    • Roh, S.; Chung, T.; Lee, B. Overview of the characteristic of micro- and nanao-structured surface plasmon resonanace. Sensors 2011, 11, 1565-1588.
    • (2011) Sensors , vol.11 , pp. 1565-1588
    • Roh, S.1    Chung, T.2    Lee, B.3
  • 40
    • 78650288422 scopus 로고    scopus 로고
    • Resolution enhacement in surface plasmon resonanace sensor based on waveguide coupled mode by combining a bimetallic approach
    • Lee, K.-S.; Son, J.M.; Jeong, D.-Y.; Lee, T.S.; Kim, W.M. Resolution enhacement in surface plasmon resonanace sensor based on waveguide coupled mode by combining a bimetallic approach. Sensors 2010, 10, 11390-11399.
    • (2010) Sensors , vol.10 , pp. 11390-11399
    • Lee, K.-S.1    Son, J.M.2    Jeong, D.-Y.3    Lee, T.S.4    Kim, W.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.