메뉴 건너뛰기




Volumn 107, Issue 36, 2010, Pages 15687-15692

Discriminating early stage aβ42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study

Author keywords

Amyloid; Nonlinear spectroscopy; REMD

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; MONOMER; AMYLOID BETA PROTEIN; PEPTIDE FRAGMENT;

EID: 77957684507     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002131107     Document Type: Article
Times cited : (39)

References (45)
  • 1
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, et al. (1987) The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325(6106):733-6.
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297(5580):353-6.
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova AT, et al. (2002) A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 99(26):16742-7.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.26 , pp. 16742-16747
    • Petkova, A.T.1
  • 4
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-beta(1-42) fibrils
    • Luhrs T, et al. (2005) 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci USA 102(48):17342-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.48 , pp. 17342-17347
    • Luhrs, T.1
  • 5
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4(1):49-60.
    • (2003) Nat Rev Neurosci , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 6
    • 0033855845 scopus 로고    scopus 로고
    • The Alzheimer's peptide a beta adopts a collapsed coil structure in water
    • Zhang S, et al. (2000) The Alzheimer's peptide a beta adopts a collapsed coil structure in water. J Struct Biol 130(2-3):130-41.
    • (2000) J Struct Biol , vol.130 , Issue.2-3 , pp. 130-141
    • Zhang, S.1
  • 8
    • 0035133048 scopus 로고    scopus 로고
    • Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution
    • Massi F, Peng JW, Lee JP, Straub JE (2001) Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. Biophys J 80(1):31-44.
    • (2001) Biophys J , vol.80 , Issue.1 , pp. 31-44
    • Massi, F.1    Peng, J.W.2    Lee, J.P.3    Straub, J.E.4
  • 9
    • 10744219665 scopus 로고    scopus 로고
    • Solution NMR studies of the Abeta(1-40) and Abeta(1-42) peptides establish that the met35 oxidation state affects the mechanism of amyloid formation
    • Hou L, et al. (2004) Solution NMR studies of the Abeta(1-40) and Abeta(1-42) peptides establish that the met35 oxidation state affects the mechanism of amyloid formation. J Am Chem Soc 126(7):1992-2005.
    • (2004) J Am Chem Soc , vol.126 , Issue.7 , pp. 1992-2005
    • Hou, L.1
  • 10
    • 0035173352 scopus 로고    scopus 로고
    • NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two alzheimer peptides with widely different plaque-competence, a beta(140)(ox) and a beta(142)(ox)
    • Riek R, Guntert P, Dobeli H, Wipf B, Wuthrich K (2001) NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two alzheimer peptides with widely different plaque-competence, a beta(1-40)(ox) and a beta(1-42)(ox). Eur J Biochem 268(22):5930-6.
    • (2001) Eur J Biochem , vol.268 , Issue.22 , pp. 5930-5936
    • Riek, R.1    Guntert, P.2    Dobeli, H.3    Wipf, B.4    Wuthrich, K.5
  • 11
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PT, Zagorski MG (1992) Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J Mol Biol 225(4):1075-93.
    • (1992) J Mol Biol , vol.225 , Issue.4 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 12
    • 66149084447 scopus 로고    scopus 로고
    • Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution
    • Shim SH, et al. (2009) Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proc Natl Acad Sci USA 106(16):6614-6619.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.16 , pp. 6614-6619
    • Shim, S.H.1
  • 13
    • 45549085028 scopus 로고    scopus 로고
    • Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from a beta 40
    • Kim YS, Liu L, Axelsen PH, Hochstrasser RM (2008) Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from A beta 40. Proc Natl Acad Sci USA 105(22):7720-7725.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.22 , pp. 7720-7725
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 14
    • 70449584579 scopus 로고    scopus 로고
    • 2D IR provides evidence for mobile water molecules in beta-amyloid fibrils
    • Kim YS, Liu L, Axelsen PH, Hochstrasser RM (2009) 2D IR provides evidence for mobile water molecules in beta-amyloid fibrils. Proc Natl Acad Sci USA 106(42):17751-17756.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.42 , pp. 17751-17756
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 15
    • 35448943588 scopus 로고    scopus 로고
    • Simulation of two-dimensional infrared spectroscopy of amyloid fibrils
    • Zhuang W, Abrarnavicius D, Voronine DV, Mukarmel S (2007) Simulation of two-dimensional infrared spectroscopy of amyloid fibrils. Proc Nat Acad Sci USA 104(36):14233-14236.
    • (2007) Proc Nat Acad Sci USA , vol.104 , Issue.36 , pp. 14233-14236
    • Zhuang, W.1    Abrarnavicius, D.2    Voronine, D.V.3    Mukarmel, S.4
  • 16
    • 23644452100 scopus 로고    scopus 로고
    • The alzheimer beta-peptide shows temperature-dependent transitions between left-handed 3-helix, beta-strand and random coil secondary structures
    • Danielsson J, Jarvet J, Damberg P, Graslund A (2005) The alzheimer beta-peptide shows temperature-dependent transitions between left-handed 3-helix, beta-strand and random coil secondary structures. Febs J 272(15):3938-49.
    • (2005) Febs J , vol.272 , Issue.15 , pp. 3938-3949
    • Danielsson, J.1    Jarvet, J.2    Damberg, P.3    Graslund, A.4
  • 17
    • 33644672979 scopus 로고    scopus 로고
    • Salmon calcitonin and amyloid beta: Two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states
    • Schweitzer-Stenner R, Measey T, Hagarman A, Eker F, Griebenow K (2006) Salmon calcitonin and amyloid beta: Two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states. Biochemistry 45(9):2810-9.
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 2810-2819
    • Schweitzer-Stenner, R.1    Measey, T.2    Hagarman, A.3    Eker, F.4    Griebenow, K.5
  • 18
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta -protein (abeta) assembly: Abeta 40 and abeta 42 oligomerize through distinct pathways
    • Bitan G, et al. (2003) Amyloid beta -protein (abeta) assembly: Abeta 40 and abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci USA 100(1):330-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.1 , pp. 330-335
    • Bitan, G.1
  • 19
    • 33751106208 scopus 로고    scopus 로고
    • Abeta42 is more rigid than Abeta40 at the c terminus: Implications for abeta aggregation and toxicity
    • Yan Y, Wang C (2006) Abeta42 is more rigid than Abeta40 at the c terminus: Implications for abeta aggregation and toxicity. J Mol Biol 364(5):853-862.
    • (2006) J Mol Biol , vol.364 , Issue.5 , pp. 853-862
    • Yan, Y.1    Wang, C.2
  • 20
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's peptides aβ40 and 42 adopt distinct conformations in water: A combined MD/NMR study
    • Sgourakis NG, Yan YL, McCallum SA, Wang CY, 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.L.2    McCallum, S.A.3    Wang, C.Y.4    Garcia, A.E.5
  • 21
    • 33645238380 scopus 로고    scopus 로고
    • The 3D profile method for identifying fibril-forming segments of proteins
    • Thompson MJ, et al. (2006) The 3D profile method for identifying fibril-forming segments of proteins. Proc Natl Acad Sci USA 103(11):4074-8.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.11 , pp. 4074-4078
    • Thompson, M.J.1
  • 22
    • 0026320866 scopus 로고
    • The energy landscape and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG (1991) The energy landscape and motions of proteins. Science 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 23
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL (2001) Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. Phys Chem B 105(28):6474-6487.
    • (2001) Phys Chem B , vol.105 , Issue.28 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 25
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, Fraaije Jgem (1997) LINCS: A linear constraint solver for molecular simulations. J Comput Chem 18(12):1463-1472.
    • (1997) J Comput Chem , vol.18 , Issue.12 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 26
    • 84986440341 scopus 로고
    • SETTLE - An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto S, Kollman PA (1992) SETTLE - An analytical version of the SHAKE and RATTLE algorithm for rigid water models. J Comput Chem 13(8):952-962.
    • (1992) J Comput Chem , vol.13 , Issue.8 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 27
    • 0003036862 scopus 로고
    • Constant temperature molecular-dynamics methods
    • Nose S (1991) Constant temperature molecular-dynamics methods. Prog Theor Phys Supp 103:1-46.
    • (1991) Prog Theor Phys Supp , vol.103 , pp. 1-46
    • Nose, S.1
  • 28
    • 27344454932 scopus 로고    scopus 로고
    • Gromacs: Fast, flexible, and free
    • Van der Spoel D, et al. (2005) Gromacs: Fast, flexible, and free. J Comput Chem 26(16):1701-1718.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1701-1718
    • Van Der Spoel, D.1
  • 30
    • 33749368925 scopus 로고    scopus 로고
    • Ultrafast carbon-carbon single-bond rotational isomerization in room-temperature solution
    • Zheng JR, Kwak KW, Xie J, Fayer MD (2006) Ultrafast carbon-carbon single-bond rotational isomerization in room-temperature solution. Science 313:1951-1955.
    • (2006) Science , vol.313 , pp. 1951-1955
    • Zheng, J.R.1    Kwak, K.W.2    Xie, J.3    Fayer, M.D.4
  • 31
    • 23844509509 scopus 로고    scopus 로고
    • Chemical exchange 2D IR of hydrogen-bond making and breaking
    • Kim YS, Hochstrasser RM (2005) Chemical exchange 2D IR of hydrogen-bond making and breaking. Proc Natl Acad Sci USA 102:11185-11190.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11185-11190
    • Kim, Y.S.1    Hochstrasser, R.M.2
  • 32
    • 33751313515 scopus 로고    scopus 로고
    • Watching hydrogen-bond dynamics in a beta-turn by transient two-dimensional infrared spectroscopy
    • Kolano C, Helbing J, Kozinski M, Sander W, Hamm P (2006) Watching hydrogen-bond dynamics in a beta-turn by transient two-dimensional infrared spectroscopy. Nature 444:469-472.
    • (2006) Nature , vol.444 , pp. 469-472
    • Kolano, C.1    Helbing, J.2    Kozinski, M.3    Sander, W.4    Hamm, P.5
  • 33
    • 70349783538 scopus 로고    scopus 로고
    • Coherent multidimensional vibrational spectroscopy of biomolecules: Concepts, simulations, and challenges
    • Zhuang W, Hayashi T, Mukamel S (2009) Coherent multidimensional vibrational spectroscopy of biomolecules: Concepts, simulations, and challenges. Angew Chem Int Edit 48:3750-3781.
    • (2009) Angew Chem Int Edit , vol.48 , pp. 3750-3781
    • Zhuang, W.1    Hayashi, T.2    Mukamel, S.3
  • 34
    • 42449110311 scopus 로고    scopus 로고
    • Amide I two-dimensional infrared spectroscopy of proteins
    • Ganim Z, et al. (2008) Amide I two-dimensional infrared spectroscopy of proteins. Accounts Chem Res 41:432-441.
    • (2008) Accounts Chem Res , vol.41 , pp. 432-441
    • Ganim, Z.1
  • 35
  • 36
    • 15844424533 scopus 로고    scopus 로고
    • Two-dimensional spectroscopy of electronic couplings in photosynthesis
    • Brixner T, et al. (2005) Two-dimensional spectroscopy of electronic couplings in photosynthesis. Nature 434:625-628.
    • (2005) Nature , vol.434 , pp. 625-628
    • Brixner, T.1
  • 38
    • 33845519291 scopus 로고    scopus 로고
    • Probing molecular chirality via excitonic nonlinear response
    • Abramavicius D, Zhuang W, Mukamel S (2006) Probing molecular chirality via excitonic nonlinear response. J Phys B-At Mol Opt 39:5051-5066.
    • (2006) J Phys B-At Mol Opt , vol.39 , pp. 5051-5066
    • Abramavicius, D.1    Zhuang, W.2    Mukamel, S.3
  • 40
    • 0030628997 scopus 로고    scopus 로고
    • Infrared and Raman Vibrational Optical Activity: Theoretical and Experimental Aspects
    • Nafie LA (1997) Infrared and Raman vibrational optical activity: Theoretical and experimental aspects. Annu Rev Phys Chem 48:357-386. (Pubitemid 127443912)
    • (1997) Annual Review of Physical Chemistry , vol.48 , Issue.1 , pp. 357-386
    • Nafie, L.A.1
  • 42
    • 33644914712 scopus 로고    scopus 로고
    • Simulation protocols for coherent femtosecond vibrational spectra of peptides
    • Zhuang W, Abramavicius D, Hayashi T, Mukamel S (2006) Simulation protocols for coherent femtosecond vibrational spectra of peptides. J Phys Chem B 108:18034-18045.
    • (2006) J Phys Chem B , vol.108 , pp. 18034-18045
    • Zhuang, W.1    Abramavicius, D.2    Hayashi, T.3    Mukamel, S.4
  • 43
    • 44949148016 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy as a probe of the solvent electrostatic field for a twelve residue peptide
    • Wang JP, Zhuang W, Mukamel S, Hochstrasser R (2008) Two-dimensional infrared spectroscopy as a probe of the solvent electrostatic field for a twelve residue peptide. J Phys Chem B 112:5930-5937.
    • (2008) J Phys Chem B , vol.112 , pp. 5930-5937
    • Wang, J.P.1    Zhuang, W.2    Mukamel, S.3    Hochstrasser, R.4
  • 44
    • 69549114733 scopus 로고    scopus 로고
    • Sensitivity of 2D IR spectra to peptide helicity: A concerted experimental and simulation study of an octapeptide
    • Sengupta N, et al. (2009) Sensitivity of 2D IR spectra to peptide helicity: A concerted experimental and simulation study of an octapeptide. J Phys Chem B 113:12037-12049.
    • (2009) J Phys Chem B , vol.113 , pp. 12037-12049
    • Sengupta, N.1
  • 45
    • 76149100211 scopus 로고    scopus 로고
    • Quantitative surface chirality detection with sum frequency generation vibrational spectroscopy: Twin polarization angle approach
    • Feng W, Xu Y, Guo Y, Liu S, Wang H (2009) Quantitative surface chirality detection with sum frequency generation vibrational spectroscopy: Twin polarization angle approach. Chin J Chem Phys 22(6):592-600.
    • (2009) Chin J Chem Phys , vol.22 , Issue.6 , pp. 592-600
    • Feng, W.1    Xu, Y.2    Guo, Y.3    Liu, S.4    Wang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.