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Volumn 42, Issue 6, 2013, Pages 487-494

Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO2 surface

Author keywords

Sheet propensity; Amyloid beta; Molecular dynamics simulation; TiO2 rutile surface

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); NANOMATERIAL; PEPTIDE; PEPTIDE FRAGMENT; TITANIUM; TITANIUM DIOXIDE;

EID: 84878526400     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-013-0900-6     Document Type: Article
Times cited : (11)

References (75)
  • 2
    • 84864222171 scopus 로고    scopus 로고
    • Amyloid-β fibril disruption by C60-molecular guidance for rational drug design
    • 10.1039/c2cp40680b 1:CAS:528:DC%2BC38Xns12juro%3D
    • Andujar SA, Lugli F, Hofinger S, Enriz RD, Zerbetto F (2012) Amyloid-β fibril disruption by C60-molecular guidance for rational drug design. Phys Chem Chem Phys 14:8599-8607
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 8599-8607
    • Andujar, S.A.1    Lugli, F.2    Hofinger, S.3    Enriz, R.D.4    Zerbetto, F.5
  • 3
    • 79957527414 scopus 로고    scopus 로고
    • Polymorphism of Amyloid β peptide in different environments: Implications for membrane insertion and pore formation
    • 21918653 10.1039/c1sm05162h 1:CAS:528:DC%2BC3MXmsVCqsbk%3D
    • Arce FT, Jang H, Ramachandran S, Landon PB, Nussinov R, Lal R (2011) Polymorphism of Amyloid β peptide in different environments: implications for membrane insertion and pore formation. Soft Matter 7:5267-5273
    • (2011) Soft Matter , vol.7 , pp. 5267-5273
    • Arce, F.T.1    Jang, H.2    Ramachandran, S.3    Landon, P.B.4    Nussinov, R.5    Lal, R.6
  • 4
    • 33846324298 scopus 로고    scopus 로고
    • The structure of the Alzheimer Amyloid β 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent
    • 17166516 10.1016/j.jmb.2006.11.015 1:CAS:528:DC%2BD2sXhtVejurw%3D
    • Baumketner A, Shea J-E (2007) The structure of the Alzheimer Amyloid β 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent. J Mol Biol 366:275-285
    • (2007) J Mol Biol , vol.366 , pp. 275-285
    • Baumketner, A.1    Shea, J.-E.2
  • 5
    • 13944282886 scopus 로고    scopus 로고
    • Amyloid β-protein: Monomer structure and early aggregation states of Aβ 42 and its Pro19 Alloform
    • 15713083 10.1021/ja044531p 1:CAS:528:DC%2BD2MXosFSqsg%3D%3D
    • Bernstein SL, Wyttenbach T, Baumketner A, Shea J-E, Bitan G, Teplow DB, Bowers MT (2005) Amyloid β-protein: monomer structure and early aggregation states of Aβ 42 and its Pro19 Alloform. J Am Chem Soc 127:2075-2084
    • (2005) J Am Chem Soc , vol.127 , pp. 2075-2084
    • Bernstein, S.L.1    Wyttenbach, T.2    Baumketner, A.3    Shea, J.-E.4    Bitan, G.5    Teplow, D.B.6    Bowers, M.T.7
  • 7
    • 46749127364 scopus 로고    scopus 로고
    • Are current molecular dynamics force fields too helical?
    • 18456823 10.1529/biophysj.108.132696 1:CAS:528:DC%2BD1cXnslWlsbo%3D
    • Best RB, Buchete N-V, Hummer G (2008) Are current molecular dynamics force fields too helical? Biophys J 95:L07-L09
    • (2008) Biophys J , vol.95
    • Best, R.B.1    Buchete, N.-V.2    Hummer, G.3
  • 8
    • 36849036973 scopus 로고    scopus 로고
    • Misfolding of amyloidogenic proteins at membrane surfaces: The impact of macromolecular crowding
    • 17990885 10.1021/ja076059o 1:CAS:528:DC%2BD2sXht12gs7vK
    • Bokvist M, Gröbner G (2007) Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecular crowding. J Am Chem Soc 129:14848-14849
    • (2007) J Am Chem Soc , vol.129 , pp. 14848-14849
    • Bokvist, M.1    Gröbner, G.2
  • 9
    • 0142027278 scopus 로고    scopus 로고
    • Molecular dynamics study of the influence of solid interfaces on poly (ethylene oxide) structure and dynamics
    • 10.1021/ma0346005 1:CAS:528:DC%2BD3sXnt1KksL0%3D
    • Borodin O, Smith GD, Bandyopadhyaya R, Byutner O (2003) Molecular dynamics study of the influence of solid interfaces on poly (ethylene oxide) structure and dynamics. Macromolecules 36:7873-7883
    • (2003) Macromolecules , vol.36 , pp. 7873-7883
    • Borodin, O.1    Smith, G.D.2    Bandyopadhyaya, R.3    Byutner, O.4
  • 10
    • 77957717046 scopus 로고    scopus 로고
    • Effects of hypericin on the structure and aggregation properties of β-amyloid peptides
    • 20473492 10.1007/s00249-010-0607-x 1:CAS:528:DC%2BC3cXht1SntrnO
    • Bramanti E, Lenci F, Sgarbossa A (2010) Effects of hypericin on the structure and aggregation properties of β-Amyloid peptides. Eur Biophys J 39:1493-1501
    • (2010) Eur Biophys J , vol.39 , pp. 1493-1501
    • Bramanti, E.1    Lenci, F.2    Sgarbossa, A.3
  • 12
    • 84986512474 scopus 로고
    • Charmm: A program for macromolecular energy, minimization, and dynamics calculations
    • 10.1002/jcc.540040211 1:CAS:528:DyaL3sXit1aiu7w%3D
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M (1983) Charmm: a program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Olafson, B.D.3    States, D.J.4    Swaminathan, S.5    Karplus, M.6
  • 13
    • 38949205552 scopus 로고    scopus 로고
    • Delineating the mechanism of Alzheimer's Disease Aβ peptide neurotoxicity
    • 17762917 10.1007/s11064-007-9469-8 1:CAS:528:DC%2BD1cXhs1ahsLk%3D
    • Cappai R, Barnham K (2008) Delineating the mechanism of Alzheimer's Disease Aβ peptide neurotoxicity. Neurochem Res 33:526-532
    • (2008) Neurochem Res , vol.33 , pp. 526-532
    • Cappai, R.1    Barnham, K.2
  • 14
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces: Models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria
    • 8913577 10.1016/S0006-3495(96)79430-4 1:CAS:528:DyaK28XmslGgsbw%3D
    • Chatelier RC, Minton AP (1996) Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria. Biophys J 71:2367-2374
    • (1996) Biophys J , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 15
    • 84860289084 scopus 로고    scopus 로고
    • Effect of the A30P mutation on the structural dynamics of micelle-bound α-synuclein released in water: A molecular dynamics study
    • 10.1007/s00249-012-0803-y 1:CAS:528:DC%2BC38Xlsl2qu70%3D
    • Chatterjee P, Sengupta N (2012) Effect of the A30P mutation on the structural dynamics of micelle-bound αSynuclein released in water: a molecular dynamics study. European Biophys J 41:483-489
    • (2012) European Biophys J , vol.41 , pp. 483-489
    • Chatterjee, P.1    Sengupta, N.2
  • 16
    • 84863969999 scopus 로고    scopus 로고
    • Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure
    • 22283547 10.1021/jp2118778 1:CAS:528:DC%2BC38XhsVWitLg%3D
    • Chebaro Y, Jiang P, Zang T, Mu Y, Nguyen PH, Mousseau N, Derreumaux P (2012) Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure. J Phys Chem B 116:8412-8422
    • (2012) J Phys Chem B , vol.116 , pp. 8412-8422
    • Chebaro, Y.1    Jiang, P.2    Zang, T.3    Mu, Y.4    Nguyen, P.H.5    Mousseau, N.6    Derreumaux, P.7
  • 17
    • 65649095786 scopus 로고    scopus 로고
    • Gold nanoparticles: From nanomedicine to nanosensing
    • 1:CAS:528:DC%2BD1cXhsFSns73P
    • Chen PC, Mwakwari SC, Oyelere AK (2008) Gold nanoparticles: from nanomedicine to nanosensing. Nanotechnol Sci Appl 1:45-66
    • (2008) Nanotechnol Sci Appl , vol.1 , pp. 45-66
    • Chen, P.C.1    Mwakwari, S.C.2    Oyelere, A.K.3
  • 18
    • 84861217855 scopus 로고    scopus 로고
    • Impact of chemical heterogeneity on protein self-assembly in water
    • 22538814 10.1073/pnas.1120646109 1:CAS:528:DC%2BC38Xot1KnsL8%3D
    • Chong S-H, Ham S (2012) Impact of chemical heterogeneity on protein self-assembly in water. Proc Natl Acad Sci USA 109:7636-7641
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 7636-7641
    • Chong, S.-H.1    Ham, S.2
  • 19
    • 34547481020 scopus 로고    scopus 로고
    • Nanoparticles as catalysts for protein fibrillation
    • 17502593 10.1073/pnas.0703194104 1:CAS:528:DC%2BD2sXmt1aktL8%3D
    • Colvin VL, Kulinowski KM (2007) Nanoparticles as catalysts for protein fibrillation. Proc Natl Acad Sci USA 104:8679-8680
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8679-8680
    • Colvin, V.L.1    Kulinowski, K.M.2
  • 20
    • 61549084018 scopus 로고    scopus 로고
    • Interaction between amyloid-β (1-42) peptide and phospholipid bilayers: A molecular dynamics study
    • 19186121 10.1016/j.bpj.2008.09.053 1:CAS:528:DC%2BD1MXnslGitbw%3D
    • Davis CH, Berkowitz ML (2009a) Interaction between amyloid-β (1-42) peptide and phospholipid bilayers: a molecular dynamics study. Biophys J 96:785-797
    • (2009) Biophys J , vol.96 , pp. 785-797
    • Davis, C.H.1    Berkowitz, M.L.2
  • 21
    • 70350397192 scopus 로고    scopus 로고
    • Structure of the amyloid-β (1-42) monomer absorbed to model phospholipid bilayers: A molecular dynamics study
    • 19807060 10.1021/jp905889z 1:CAS:528:DC%2BD1MXht1ahtbjP
    • Davis CH, Berkowitz ML (2009b) Structure of the amyloid-β (1-42) monomer absorbed to model phospholipid bilayers: a molecular dynamics study. J Phys Chem B 113:14480-14486
    • (2009) J Phys Chem B , vol.113 , pp. 14480-14486
    • Davis, C.H.1    Berkowitz, M.L.2
  • 22
    • 51049090204 scopus 로고    scopus 로고
    • Nanoparticle therapeutics: An emerging treatment modality for cancer
    • 10.1038/nrd2614 1:CAS:528:DC%2BD1cXhtVGgtL%2FJ
    • Davis ME, Chen Z, Shin DM (2008) Nanoparticle therapeutics: an emerging treatment modality for cancer. Natl Rev Drug Discov 7:771-782
    • (2008) Natl Rev Drug Discov , vol.7 , pp. 771-782
    • Davis, M.E.1    Chen, Z.2    Shin, D.M.3
  • 23
    • 77952094986 scopus 로고    scopus 로고
    • Beta amyloid peptide: From different aggregation forms to the activation of different biochemical pathways
    • 10.1007/s00249-009-0439-8
    • Di Carlo M (2010) Beta amyloid peptide: from different aggregation forms to the activation of different biochemical pathways. Euro Biophys J 39:877-888
    • (2010) Euro Biophys J , vol.39 , pp. 877-888
    • Di Carlo, M.1
  • 24
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid β-protein fibril assembly
    • 12149256 10.1074/jbc.M204168200 1:CAS:528:DC%2BD38XnsVaqtrk%3D
    • Fezoui Y, Teplow DB (2002) Kinetic studies of amyloid β-protein fibril assembly. J Biol Chem 277:36948-36954
    • (2002) J Biol Chem , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 25
    • 70350028289 scopus 로고    scopus 로고
    • Induced β-barrel formation of the Alzheimer's Aβ25-35 oligomers on carbon nanotube surfaces: Implication for amyloid fibril inhibition
    • 10.1016/j.bpj.2009.07.014
    • Fu Z, Luo Y, Derreumaux P, Wei G (2009) Induced β-barrel formation of the Alzheimer's Aβ25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition. Biophys J 97:1803-1975
    • (2009) Biophys J , vol.97 , pp. 1803-1975
    • Fu, Z.1    Luo, Y.2    Derreumaux, P.3    Wei, G.4
  • 26
    • 20444488480 scopus 로고    scopus 로고
    • Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces
    • 15889393 10.1002/mabi.200400189 1:CAS:528:DC%2BD2MXkslyrtbY%3D
    • Giacomelli CE, Norde W (2005) Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces. Macromol Biosci 5:401-407
    • (2005) Macromol Biosci , vol.5 , pp. 401-407
    • Giacomelli, C.E.1    Norde, W.2
  • 27
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • 17428603 10.1016/j.pneurobio.2007.02.001 1:CAS:528:DC%2BD2sXlt1arsrw%3D
    • Gralle M, Ferreira ST (2007) Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. Prog Neurobiol 82:11-32
    • (2007) Prog Neurobiol , vol.82 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 28
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • 17245412 10.1038/nrm2101 1:CAS:528:DC%2BD2sXotFKmtw%3D%3D
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8:101-112
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 30
    • 49049098668 scopus 로고    scopus 로고
    • Thermodynamic and kinetic origins of Alzheimer's and related diseases: A chemical engineer's perspective
    • 10.1002/aic.11589 1:CAS:528:DC%2BD1cXovFejtb4%3D
    • Hall CK (2008) Thermodynamic and kinetic origins of Alzheimer's and related diseases: a chemical engineer's perspective. AIChE J 54:1956-1962
    • (2008) AIChE J , vol.54 , pp. 1956-1962
    • Hall, C.K.1
  • 31
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • 12130773 10.1126/science.1072994 1:CAS:528:DC%2BD38Xls1Cju7s%3D
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 32
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 8744570 10.1016/0263-7855(96)00018-5 1:CAS:528:DyaK28Xis12nsrg%3D
    • Humphrey W, Dalke A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14:33-38
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 33
    • 84859912407 scopus 로고    scopus 로고
    • 1-42 on the surface of a single-walled carbon nanotube: A molecular dynamics simulation study
    • 22768945 10.1016/j.bpj.2012.03.036 1:CAS:528:DC%2BC38XmtVektro%3D
    • 1-42 on the surface of a single-walled carbon nanotube: a molecular dynamics simulation study. Biophys J 102:1889-1896
    • (2012) Biophys J , vol.102 , pp. 1889-1896
    • Jana, A.K.1    Sengupta, N.2
  • 34
    • 84871319339 scopus 로고    scopus 로고
    • Critical roles of key domains in complete adsorption of Aβ peptide on single-walled carbon nanotubes: Insights with point mutations and MD simulations
    • 23203213 10.1039/c2cp42933k 1:CAS:528:DC%2BC38XhvVajsrfM
    • Jana AK, Jose JC, Sengupta N (2013) Critical roles of key domains in complete adsorption of Aβ peptide on single-walled carbon nanotubes: insights with point mutations and MD simulations. Phys Chem Chem Phys 15:837-844
    • (2013) Phys Chem Chem Phys , vol.15 , pp. 837-844
    • Jana, A.K.1    Jose, J.C.2    Sengupta, N.3
  • 35
    • 84863240972 scopus 로고    scopus 로고
    • Enrichment of amyloidogenesis at an air-water interface
    • 22404938 10.1016/j.bpj.2012.01.041 1:CAS:528:DC%2BC38XjsFOntLg%3D
    • Jean L, Lee Chiu F, Vaux David J (2012) Enrichment of amyloidogenesis at an air-water interface. Biophys J 102:1154-1162
    • (2012) Biophys J , vol.102 , pp. 1154-1162
    • Jean, L.1    Lee Chiu, F.2    Vaux David, J.3
  • 38
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 12702875 10.1126/science.1079469 1:CAS:528:DC%2BD3sXivFyms7k%3D
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 39
    • 84877157835 scopus 로고    scopus 로고
    • Binding to the lipid monolayer induces conformational transition in Aβ monomer
    • doi: 10.1007/s00894-012-1596-8
    • Kim S, Klimov D (2012) Binding to the lipid monolayer induces conformational transition in Aβ monomer. J Mol Mod. doi: 10.1007/s00894-012-1596-8
    • (2012) J Mol Mod.
    • Kim, S.1    Klimov, D.2
  • 40
    • 0037418703 scopus 로고    scopus 로고
    • Fullerene inhibits β-amyloid peptide aggregation
    • 12659858 10.1016/S0006-291X(03)00393-0 1:CAS:528:DC%2BD3sXitlWht7Y%3D
    • Kim JE, Lee M (2003) Fullerene inhibits β-amyloid peptide aggregation. Biochem Biophys Res Commun 303:576-579
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 576-579
    • Kim, J.E.1    Lee, M.2
  • 42
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • 10097098 10.1073/pnas.96.7.3688 1:CAS:528:DyaK1MXjslCiurk%3D
    • Kowalewski T, Holtzman DM (1999) In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: new insights into mechanism of β-sheet formation. Proc Natl Acad Sci USA 96:3688-3693
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 43
    • 84871575381 scopus 로고    scopus 로고
    • Using nanoscale substrate curvature to control the dimerization of a surface-bound protein
    • doi: 10.1021/nn302948d
    • Kurylowicz M, Giuliani M, Dutcher JR (2012) Using nanoscale substrate curvature to control the dimerization of a surface-bound protein. ACS Nano doi: 10.1021/nn302948d
    • (2012) ACS Nano
    • Kurylowicz, M.1    Giuliani, M.2    Dutcher, J.R.3
  • 44
    • 34248208920 scopus 로고    scopus 로고
    • Carbon nanotubes as nanomedicines: From toxicology to pharmacology
    • 17113677 10.1016/j.addr.2006.09.015 1:CAS:528:DC%2BD28Xht1KmtLbN
    • Lacerda L, Bianco A, Prato M, Kostarelos K (2006) Carbon nanotubes as nanomedicines: from toxicology to pharmacology. Adv Drug Deliv Rev 58:1460-1470
    • (2006) Adv Drug Deliv Rev , vol.58 , pp. 1460-1470
    • Lacerda, L.1    Bianco, A.2    Prato, M.3    Kostarelos, K.4
  • 45
    • 78650086243 scopus 로고    scopus 로고
    • Characterizing amyloid-beta protein misfolding from molecular dynamics simulations with explicit water
    • 20734314 10.1002/jcc.21628
    • Lee C, Ham S (2010) Characterizing amyloid-beta protein misfolding from molecular dynamics simulations with explicit water. J Comput Chem 32:349-355
    • (2010) J Comput Chem , vol.32 , pp. 349-355
    • Lee, C.1    Ham, S.2
  • 46
    • 84868325436 scopus 로고    scopus 로고
    • Combined effects of agitation, macromolecular crowding and interfaces on amyloidogenesis
    • doi: 10.1074/jbc.M112.400580
    • Lee CF, Bird S, Shaw M, Jean L, Vaux DJ (2012) Combined effects of agitation, macromolecular crowding and interfaces on amyloidogenesis. J Biol Chem. doi: 10.1074/jbc.M112.400580
    • (2012) J Biol Chem.
    • Lee, C.F.1    Bird, S.2    Shaw, M.3    Jean, L.4    Vaux, D.J.5
  • 47
    • 33947182575 scopus 로고    scopus 로고
    • The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides
    • 17328898 10.1016/j.febslet.2007.02.026 1:CAS:528:DC%2BD2sXjtFGrtrs%3D
    • Liao MQ, Tzeng YJ, Chang LYX, Huang HB, Lin TH, Chyan CL, Chen YC (2007) The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides. FEBS Lett 581:1161-1165
    • (2007) FEBS Lett , vol.581 , pp. 1161-1165
    • Liao, M.Q.1    Tzeng, Y.J.2    Chang, L.Y.X.3    Huang, H.B.4    Lin, T.H.5    Chyan, C.L.6    Chen, Y.C.7
  • 49
    • 79952675434 scopus 로고    scopus 로고
    • Free-energy landscape of the helical wrapping of a carbon nanotube by a polysaccharide
    • 10.1021/jp111981y 1:CAS:528:DC%2BC3MXjvFGntw%3D%3D
    • Liu Y, Chipot C, Shao X, Cai W (2011) Free-energy landscape of the helical wrapping of a carbon nanotube by a polysaccharide. J Phys Chem C 115:1851-1856
    • (2011) J Phys Chem C , vol.115 , pp. 1851-1856
    • Liu, Y.1    Chipot, C.2    Shao, X.3    Cai, W.4
  • 50
    • 34547362096 scopus 로고    scopus 로고
    • Dendrimer-mediated synthesis of water-dispersible carbon-nanotube- supported oxide nanoparticles
    • 10.1021/jp0702999 1:CAS:528:DC%2BD2sXlvVWjt7k%3D
    • Lu X, Imae T (2007) Dendrimer-mediated synthesis of water-dispersible carbon-nanotube-supported oxide nanoparticles. J Phys Chem C 111:8459-8462
    • (2007) J Phys Chem C , vol.111 , pp. 8459-8462
    • Lu, X.1    Imae, T.2
  • 52
    • 77954892793 scopus 로고    scopus 로고
    • Polymorphism in Alzheimer β amyloid organization reflects conformational selection in a rugged energy landscape
    • 20402519 10.1021/cr900377t 1:CAS:528:DC%2BC3cXkvFaqtbo%3D
    • Miller Y, Ma B, Nussinov R (2010) Polymorphism in Alzheimer β amyloid organization reflects conformational selection in a rugged energy landscape. Chem Rev 110:4820-4838
    • (2010) Chem Rev , vol.110 , pp. 4820-4838
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 53
    • 0032905175 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics
    • 9876132 10.1016/S0006-3495(99)77187-0 1:CAS:528:DyaK1MXjsFOjuw%3D%3D
    • Minton AP (1999) Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics. Biophys J 76:176-187
    • (1999) Biophys J , vol.76 , pp. 176-187
    • Minton, A.P.1
  • 54
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • 11279227 10.1074/jbc.R100005200 1:CAS:528:DC%2BD3MXjvFCqtr8%3D
    • Minton AP (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 276:10577-10580
    • (2001) J Biol Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 55
    • 20644449471 scopus 로고    scopus 로고
    • Modification of the generalized born model suitable for macromolecules
    • 10.1021/jp994072s 1:CAS:528:DC%2BD3cXhvVGit70%3D
    • Onufriev A, Bashford D, Case DA (2000) Modification of the generalized born model suitable for macromolecules. J Phys Chem B 104:3712-3720
    • (2000) J Phys Chem B , vol.104 , pp. 3712-3720
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 56
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • 10.1002/prot.20033 1:CAS:528:DC%2BD2cXjtFKhs78%3D
    • Onufriev A, Bashford D, Case DA (2004) Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins Struct Func Bioinf 55:383-394
    • (2004) Proteins Struct Func Bioinf , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 57
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • 11509390 10.1016/S0006-3495(01)75831-6 1:CAS:528:DC%2BD3MXmtlCkur8%3D
    • Pallitto MM, Murphy RM (2001) A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state. Biophys J 81:1805-1822
    • (2001) Biophys J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 58
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • 19376973 10.1073/pnas.0812033106 1:CAS:528:DC%2BD1MXmt1Khtro%3D
    • Paravastu AK, Qahwash I, Leapman RD, Meredith SC, Tycko R (2009) Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc Natl Acad Sci USA 106:7443-7448
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 59
    • 70349587461 scopus 로고    scopus 로고
    • On the stability of the soluble amyloid aggregates
    • 19720034 10.1016/j.bpj.2009.05.055 1:CAS:528:DC%2BD1MXhsVCjsrjN
    • Sahoo B, Nag S, Sengupta P, Maiti S (2009) On the stability of the soluble amyloid aggregates. Biophys J 97:1454-1460
    • (2009) Biophys J , vol.97 , pp. 1454-1460
    • Sahoo, B.1    Nag, S.2    Sengupta, P.3    Maiti, S.4
  • 60
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: A combined MD/NMR study
    • 17397862 10.1016/j.jmb.2007.02.093 1:CAS:528:DC%2BD2sXkslCmsLg%3D
    • Sgourakis NG, Yan Y, McCallum SA, Wang C, Garcia AE (2007) The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: a combined MD/NMR study. J Mol Biol 368:1448-1457
    • (2007) J Mol Biol , vol.368 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.2    McCallum, S.A.3    Wang, C.4    Garcia, A.E.5
  • 61
    • 84862867927 scopus 로고    scopus 로고
    • Molecular interaction of proteins and peptides with nanoparticles
    • 22621430 10.1021/nn300415x 1:CAS:528:DC%2BC38XnsVKrsb8%3D
    • Shemetov AA, Nabiev I, Sukhanova A (2012) Molecular interaction of proteins and peptides with nanoparticles. ACS Nano 6:4585-4602
    • (2012) ACS Nano , vol.6 , pp. 4585-4602
    • Shemetov, A.A.1    Nabiev, I.2    Sukhanova, A.3
  • 62
    • 32344451179 scopus 로고    scopus 로고
    • The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of beta conformation seeding
    • 10.1002/cbic.200500223
    • Simona T, Veronica E, Paolo V, Nico AJvN, Alexandre MJJB, Remo G, Teodorico T, Piero AT, Delia P (2006) The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding. Chembiochem 7:257-267
    • (2006) Chembiochem , vol.7 , pp. 257-267
    • Simona, T.1    Veronica, E.2    Paolo, V.3    Nico, A.4    Alexandre, M.5    Remo, G.6    Teodorico, T.7    Piero, A.T.8    Delia, P.9
  • 63
    • 78650241810 scopus 로고    scopus 로고
    • Interactions of amyloid Aβ(1-42) peptide with self-assembled peptide nanospheres
    • 20814889 10.1002/psc.1284 1:CAS:528:DC%2BC3cXhsFyjtb%2FF
    • Smoak EM, Dabakis MP, Henricus MM, Tamayev R, Banerjee IA (2011) Interactions of amyloid Aβ(1-42) peptide with self-assembled peptide nanospheres. J Pept Sci 17:14-23
    • (2011) J Pept Sci , vol.17 , pp. 14-23
    • Smoak, E.M.1    Dabakis, M.P.2    Henricus, M.M.3    Tamayev, R.4    Banerjee, I.A.5
  • 64
    • 84866563494 scopus 로고    scopus 로고
    • Alzheimer Aβ peptide interactions with lipid membranes: Fibrils, oligomers and polymorphic amyloid channels
    • 22874669 10.4161/pri.21022 1:CAS:528:DC%2BC3sXisVSit70%3D
    • Tofoleanu F, Buchete N-V (2012a) Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels. Prion 6:339-345
    • (2012) Prion , vol.6 , pp. 339-345
    • Tofoleanu, F.1    Buchete, N.-V.2
  • 65
    • 84862889934 scopus 로고    scopus 로고
    • Molecular interaction of Alzheimer's AB protofilaments with lipid membranes
    • 22281438 10.1016/j.jmb.2011.12.063 1:CAS:528:DC%2BC38XhvVyjsL0%3D
    • Tofoleanu F, Buchete N-V (2012b) Molecular interaction of Alzheimer's AB protofilaments with lipid membranes. J Mol Biol 421:572-586
    • (2012) J Mol Biol , vol.421 , pp. 572-586
    • Tofoleanu, F.1    Buchete, N.-V.2
  • 67
    • 80054933491 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the adsorption of bone morphogenetic protein-2 on surfaces with medical relevance
    • 21958113 10.1021/la202489w 1:CAS:528:DC%2BC3MXht1yqu7bM
    • Utesch T, Daminelli G, Mroginski MA (2011) Molecular dynamics simulations of the adsorption of bone morphogenetic protein-2 on surfaces with medical relevance. Langmuir 27:13144-13153
    • (2011) Langmuir , vol.27 , pp. 13144-13153
    • Utesch, T.1    Daminelli, G.2    Mroginski, M.A.3
  • 68
    • 33846784849 scopus 로고    scopus 로고
    • The role of surfactants in dispersion of carbon nanotubes
    • 10.1016/j.cis.2006.11.007
    • Vaisman L, Wagner HD, Marom G (2006) The role of surfactants in dispersion of carbon nanotubes. Adv Colloid Interf Sci 128-130:37-46
    • (2006) Adv Colloid Interf Sci , vol.128-130 , pp. 37-46
    • Vaisman, L.1    Wagner, H.D.2    Marom, G.3
  • 69
    • 79958204688 scopus 로고    scopus 로고
    • Inhibition of aggregation of amyloid peptides by β-sheet breaker peptides and their binding affinity
    • 21563780 10.1021/jp1116728 1:CAS:528:DC%2BC3MXlvFClsrc%3D
    • Viet MH, Ngo ST, Lam NS, Li MS (2011) Inhibition of aggregation of amyloid peptides by β-sheet breaker peptides and their binding affinity. J Phys Chem B 115:7433-7446
    • (2011) J Phys Chem B , vol.115 , pp. 7433-7446
    • Viet, M.H.1    Ngo, S.T.2    Lam, N.S.3    Li, M.S.4
  • 70
    • 77955043921 scopus 로고    scopus 로고
    • Alzheimer Aβ 1-42 monomer adsorbed on the self-assembled monolayers
    • 20597530 10.1021/la1017906 1:CAS:528:DC%2BC3cXot1Git7g%3D
    • Wang Q, Zhao J, Yu X, Zhao C, Li L, Zheng J (2010) Alzheimer Aβ 1-42 monomer adsorbed on the self-assembled monolayers. Langmuir 26:12722-12732
    • (2010) Langmuir , vol.26 , pp. 12722-12732
    • Wang, Q.1    Zhao, J.2    Yu, X.3    Zhao, C.4    Li, L.5    Zheng, J.6
  • 71
    • 34748900551 scopus 로고    scopus 로고
    • Carbon nanotubes for biological and biomedical applications
    • 10.1088/0957-4484/18/41/412001
    • Wenrong Y, Thordarson P, Gooding JJ, Ringer SP, Braet F (2007) Carbon nanotubes for biological and biomedical applications. Nanotechnology 18:412001-412013
    • (2007) Nanotechnology , vol.18 , pp. 412001-412013
    • Wenrong, Y.1    Thordarson, P.2    Gooding, J.J.3    Ringer, S.P.4    Braet, F.5
  • 74
    • 84860112219 scopus 로고    scopus 로고
    • Structure, orientation, and surface interaction of Alzheimer amyloid-β peptides on the graphite
    • 10.1021/la3002306 1:CAS:528:DC%2BC38XkvVKms7o%3D
    • Yu X, Wang Q, Lin Y, Zhao J, Zhao C, Zheng J (2012) Structure, orientation, and surface interaction of Alzheimer amyloid-β peptides on the graphite. Langmuir 28:6595-6605
    • (2012) Langmuir , vol.28 , pp. 6595-6605
    • Yu, X.1    Wang, Q.2    Lin, Y.3    Zhao, J.4    Zhao, C.5    Zheng, J.6
  • 75
    • 83455238649 scopus 로고    scopus 로고
    • Molecular dynamics simulations of low-ordered Alzheimer β-amyloid oligomers from dimer to hexamer on self-assembled monolayers
    • 22077332 10.1021/la2027913 1:CAS:528:DC%2BC3MXhsVKiu73K
    • Zhao J, Wang Q, Liang G, Zheng J (2011) Molecular dynamics simulations of low-ordered Alzheimer β-amyloid oligomers from dimer to hexamer on self-assembled monolayers. Langmuir 27:14876-14887
    • (2011) Langmuir , vol.27 , pp. 14876-14887
    • Zhao, J.1    Wang, Q.2    Liang, G.3    Zheng, J.4


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