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Volumn 6, Issue 1, 2012, Pages 26-31

Insights into the disparate action of osmolytes and macromolecular crowders on amyloid formation

Author keywords

Amyloid fibrils; Fibril breakage; Macromolecular crowding; Osmolytes; Osmotic pressure; Protein aggregation kinetics; Protein stabilization

Indexed keywords

AMYLOID; MACROGOL; MONOMER; SORBITOL;

EID: 84857220268     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.6.1.18132     Document Type: Note
Times cited : (23)

References (40)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • PMID:14685248
    • Dobson CM. Protein folding and misfolding. Nature 2003; 426:884-90; PMID:14685248; http://dx.doi.org/10.1038/nature02261.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 48149108245 scopus 로고    scopus 로고
    • Protein aggregation in the brain: The molecular basis for alzheimer's and parkinson's diseases
    • PMID:18368143
    • Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM. Protein aggregation in the brain: The molecular basis for alzheimer's and parkinson's diseases. Mol Med 2008; 14:451-64; PMID:18368143; http://dx.doi.org/10.2119/2007-00100.Irvine.
    • (2008) Mol Med , vol.14 , pp. 451-464
    • Irvine, G.B.1    El-Agnaf, O.M.2    Shankar, G.M.3    Walsh, D.M.4
  • 3
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • PMID:16481071
    • Glabe CG. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 2006; 27:570-5; PMID:16481071; http://dx.doi.org/10.1016/j.neurobiolaging.2005.04.017.
    • (2006) Neurobiol Aging , vol.27 , pp. 570-575
    • Glabe, C.G.1
  • 4
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • PMID:10899428
    • Serpell LC. Alzheimer's amyloid fibrils: Structure and assembly. Biochim Biophys Acta 2000; 1502:16-30; PMID:10899428.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 5
    • 77955273305 scopus 로고    scopus 로고
    • Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated
    • PMID:20600131
    • Kodali R, Williams AD, Chemuru S, Wetzel R. Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated. J Mol Biol 2010; 401:503-17; PMID:20600131; http://dx.doi.org/10. 1016/j.jmb.2010.06.023.
    • (2010) J Mol Biol , vol.401 , pp. 503-517
    • Kodali, R.1    Williams, A.D.2    Chemuru, S.3    Wetzel, R.4
  • 6
    • 33947103491 scopus 로고    scopus 로고
    • Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: Insights into the effect of ph on protein fibrillogenesis
    • PMID:17320902
    • Picotti P, De Franceschi G, Frare E, Spolaore B, Zambonin M, Chiti F, et al. Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: Insights into the effect of ph on protein fibrillogenesis. J Mol Biol 2007; 367:1237-45; PMID:17320902; http://dx.doi.org/10.1016/j.jmb.2007.01. 072.
    • (2007) J Mol Biol , vol.367 , pp. 1237-1245
    • Picotti, P.1    De Franceschi, G.2    Frare, E.3    Spolaore, B.4    Zambonin, M.5    Chiti, F.6
  • 7
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • PMID:15155566
    • De Felice FG, Vieira MNN, Meirelles MNL, Morozova-Roche LA, Dobson CM, Ferreira ST. Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. FASEB J 2004; 18:1099-101; PMID:15155566.
    • (2004) FASEB J , vol.18 , pp. 1099-1101
    • De Felice, F.G.1    Vieira, M.N.N.2    Meirelles, M.N.L.3    Morozova-Roche, L.A.4    Dobson, C.M.5    Ferreira, S.T.6
  • 8
    • 33645999511 scopus 로고
    • On interaction between two bodies immersed in a solution of macromolecules
    • Asakura S, Oosawa F. On interaction between two bodies immersed in a solution of macromolecules. J Chem Phys 1954; 22:1255-6; http://dx.doi.org/10. 1063/1.1740347.
    • (1954) J Chem Phys , vol.22 , pp. 1255-1256
    • Asakura, S.1    Oosawa, F.2
  • 9
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical and potential physiological consequences
    • PMID:18573087
    • Zhou HX, Rivas G, Minton AP. Macromolecular crowding and confinement: Biochemical, biophysical and potential physiological consequences. Annu Rev Biophys 2008; 37:375-97; PMID:18573087; http://dx.doi.org/10.1146/annurev. biophys.37.032807.125817.
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 10
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • PMID:7112124
    • Yancey PH, Clark ME, Hand SC, Bowlus RD, Somero GN. Living with water stress: Evolution of osmolyte systems. Science 1982; 217:1214-22; PMID:7112124; http://dx.doi.org/10.1126/science.7112124.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 11
    • 27744555656 scopus 로고    scopus 로고
    • Protein folding, stability and solvation structure in osmolyte solutions
    • PMID:16113118
    • Rösgen J, Pettitt BM, Bolen DW. Protein folding, stability and solvation structure in osmolyte solutions. Biophys J 2005; 89:2988-97; PMID:16113118; http://dx.doi.org/10.1529/biophysj.105.067330.
    • (2005) Biophys J , vol.89 , pp. 2988-2997
    • Rösgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 13
    • 35448999589 scopus 로고    scopus 로고
    • A practical guide on how osmolytes modulate macromolecular properties
    • PMID:17964947
    • Harries D, Rösgen J. A practical guide on how osmolytes modulate macromolecular properties. Methods Cell Biol 2008; 84:679-735; PMID:17964947; http://dx.doi.org/10.1016/S0091-679X(07)84022-2.
    • (2008) Methods Cell Biol , vol.84 , pp. 679-735
    • Harries, D.1    Rösgen, J.2
  • 14
    • 77956022419 scopus 로고    scopus 로고
    • Enthalpically driven peptide stabilization by protective osmolytes
    • Camb PMID:20657920
    • Politi R, Harries D. Enthalpically driven peptide stabilization by protective osmolytes. Chem Commun (Camb) 2010; 46:6449-51; PMID:20657920; http://dx.doi.org/10.1039/c0cc01763a.
    • (2010) Chem Commun , vol.46 , pp. 6449-6451
    • Politi, R.1    Harries, D.2
  • 15
    • 16344389134 scopus 로고    scopus 로고
    • Molecular crowding enhances native state stability and refolding rates of globular proteins
    • PMID:15781864
    • Cheung MS, Klimov D, Thirumalai D. Molecular crowding enhances native state stability and refolding rates of globular proteins. Proc Natl Acad Sci USA 2005; 102:4753-8; PMID:15781864; http://dx.doi.org/10.1073/pnas.0409630102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4753-4758
    • Cheung, M.S.1    Klimov, D.2    Thirumalai, D.3
  • 16
    • 1842473533 scopus 로고    scopus 로고
    • Osmolyte-induced changes in protein conformational equilibria
    • PMID:10685050
    • Saunders AJ, Davis-Searles PR, Allen DL, Pielak GJ, Erie DA. Osmolyte-induced changes in protein conformational equilibria. Biopolymers 2000; 53:293-307; PMID:10685050; http://dx.doi.org/10.1002/(SICI)1097-0282(20000405) 53:4〈293::AID-BIP2〉3.0.CO;2-T.
    • (2000) Biopolymers , vol.53 , pp. 293-307
    • Saunders, A.J.1    Davis-Searles, P.R.2    Allen, D.L.3    Pielak, G.J.4    Erie, D.A.5
  • 17
    • 0034635965 scopus 로고    scopus 로고
    • Osmotic stress, crowding, preferential hydration and binding: A comparison of perspectives
    • PMID:10760270
    • Parsegian VA, Rand RP, Rau DC. Osmotic stress, crowding, preferential hydration and binding: A comparison of perspectives. Proc Natl Acad Sci USA 2000; 97:3987-92; PMID:10760270; http://dx.doi.org/10.1073/pnas.97.8.3987.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3987-3992
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 18
    • 3142655877 scopus 로고    scopus 로고
    • Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface†
    • PMID:15248785
    • Felitsky DJ, Record MT. Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface†. Biochemistry 2004; 43:9276-88; PMID:15248785; http://dx.doi.org/10.1021/bi049862t.
    • (2004) Biochemistry , vol.43 , pp. 9276-9288
    • Felitsky, D.J.1    Record, M.T.2
  • 19
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • PMID:12097640
    • Timasheff SN. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc Natl Acad Sci USA 2002; 99:9721-6; PMID:12097640; http://dx.doi.org/10. 1073/pnas.122225399.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 20
    • 79251538929 scopus 로고    scopus 로고
    • Crowding alone cannot account for cosolute effect on amyloid aggregation
    • PMID:21249221
    • Sukenik S, Politi R, Ziserman L, Danino D, Friedler A, Harries D. Crowding alone cannot account for cosolute effect on amyloid aggregation. PLoS ONE 2011; 6:15608; PMID:21249221; http://dx.doi.org/10.1371/journal.pone. 0015608.
    • (2011) PLoS ONE , vol.6 , pp. 15608
    • Sukenik, S.1    Politi, R.2    Ziserman, L.3    Danino, D.4    Friedler, A.5    Harries, D.6
  • 23
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • PMID:16899544
    • Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci USA 2006; 103:13357-61; PMID:16899544; http://dx.doi.org/10.1073/pnas.0603772103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 24
    • 33745922350 scopus 로고    scopus 로고
    • Cyclohexanehexol inhibitors of abeta aggregation prevent and reverse alzheimer phenotype in a mouse model
    • PMID:16767098
    • McLaurin J, Kierstead ME, Brown ME, Hawkes CA, Lambermon MH, Phinney AL, et al. Cyclohexanehexol inhibitors of abeta aggregation prevent and reverse alzheimer phenotype in a mouse model. Nat Med 2006; 12:801-8; PMID:16767098; http://dx.doi.org/10.1038/nm1423.
    • (2006) Nat Med , vol.12 , pp. 801-808
    • McLaurin, J.1    Kierstead, M.E.2    Brown, M.E.3    Hawkes, C.A.4    Lambermon, M.H.5    Phinney, A.L.6
  • 25
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges
    • PMID:12878031
    • Hall D, Minton AP. Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges. Biochim Biophys Acta 2003; 1649:127-39; PMID:12878031.
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 26
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein c-ii
    • PMID:11751863
    • Hatters DM, Minton AP, Howlett GJ. Macromolecular crowding accelerates amyloid formation by human apolipoprotein c-ii. J Biol Chem 2002; 277:7824-30; PMID:11751863; http://dx.doi.org/10.1074/jbc.M110429200.
    • (2002) J Biol Chem , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 27
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • PMID:20007899
    • Knowles TPJ, Waudby CA, Devlin GL, Cohen SIA, Aguzzi A, Vendruscolo M, et al. An analytical solution to the kinetics of breakable filament assembly. Science 2009; 326:1533-7; PMID:20007899; http://dx.doi.org/10.1126/science. 1178250.
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1    Waudby, C.A.2    Devlin, G.L.3    Cohen, S.I.A.4    Aguzzi, A.5    Vendruscolo, M.6
  • 28
    • 0032507251 scopus 로고    scopus 로고
    • Origin of β-hairpin stability in solution: Structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilization in water
    • Maynard AJ, Sharman GJ, Searle MS. Origin of β-hairpin stability in solution: Structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilization in water. J Am Chem Soc 1998; 120:1996-2007; http://dx.doi.org/10.1021/ja9726769.
    • (1998) J Am Chem Soc , vol.120 , pp. 1996-2007
    • Maynard, A.J.1    Sharman, G.J.2    Searle, M.S.3
  • 29
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism and curve-fitting: A review of the literature
    • Morris AM, Watzky Ma, Finke RG. Protein aggregation kinetics, mechanism and curve-fitting: A review of the literature. Biochim Biophys Acta 2009; 1794:375-97.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.2    Finke, R.G.3
  • 30
    • 77949278013 scopus 로고    scopus 로고
    • Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters
    • PMID:20305394
    • Xue WF, Hellewell AL, Hewitt EW, Radford SE. Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters. Prion 2010; 4:20; PMID:20305394; http://dx.doi.org/10.4161/pri.4.1.11378.
    • (2010) Prion , vol.4 , pp. 20
    • Xue, W.F.1    Hellewell, A.L.2    Hewitt, E.W.3    Radford, S.E.4
  • 31
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • PMID:18579777
    • Xue WF, Homans SW, Radford SE. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 2008; 105:8926-31; PMID:18579777; http://dx.doi.org/10.1073/pnas.0711664105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 32
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • PMID:16810177
    • Tanaka M, Collins SR, Toyama BH, Weissman JS. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585-9; PMID:16810177; http://dx.doi.org/10.1038/nature04922.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 33
    • 0002606725 scopus 로고
    • A new method of constrained optimization and a comparison with other methods
    • Box M. A new method of constrained optimization and a comparison with other methods. Comput J 1965; 8:42.
    • (1965) Comput J , vol.8 , pp. 42
    • Box, M.1
  • 34
    • 0000238336 scopus 로고
    • A simplex method for function minimization
    • Nelder JA, Mead R. A simplex method for function minimization. Comput J 1965; 7:308.
    • (1965) Comput J , vol.7 , pp. 308
    • Nelder, J.A.1    Mead, R.2
  • 35
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • PMID:16169975
    • Calamai M, Chiti F, Dobson CM. Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys J 2005; 89:4201-10; PMID:16169975; http://dx.doi.org/10.1529/biophysj.105.068726.
    • (2005) Biophys J , vol.89 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 36
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • PMID:14268785
    • Wyman J. Linked functions and reciprocal effects in hemoglobin: A second look. Adv Protein Chem 1964; 19:223-86; PMID:14268785; http://dx.doi.org/10. 1016/S0065-3233(08)60190-4.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 37
    • 79961215482 scopus 로고    scopus 로고
    • Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability
    • PMID:21742980
    • Knowles DB, Lacroix AS, Deines NF, Shkel I, Record MT. Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability. Proc Natl Acad Sci USA 2011; 108:12699-704; PMID:21742980; http://dx.doi.org/10.1073/pnas.1103382108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12699-12704
    • Knowles, D.B.1    Lacroix, A.S.2    Deines, N.F.3    Shkel, I.4    Record, M.T.5
  • 38
    • 67649515630 scopus 로고    scopus 로고
    • The impact of polyols on water structure in solution: A computational study
    • PMID:19432403
    • Politi R, Sapir L, Harries D. The impact of polyols on water structure in solution: A computational study. J Phys Chem A 2009; 113:7548-55; PMID:19432403; http://dx.doi.org/10.1021/jp9010026.
    • (2009) J Phys Chem A , vol.113 , pp. 7548-7555
    • Politi, R.1    Sapir, L.2    Harries, D.3
  • 39
    • 79251567055 scopus 로고    scopus 로고
    • Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in alzheimer's disease
    • PMID:21273426
    • Streltsov VA, Varghese JN, Masters CL, Nuttall SD. Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in alzheimer's disease. J Neurosci 2011; 31:1419-26; PMID:21273426; http://dx.doi.org/10.1523/JNEUROSCI.4259-10.2011.
    • (2011) J Neurosci , vol.31 , pp. 1419-1426
    • Streltsov, V.A.1    Varghese, J.N.2    Masters, C.L.3    Nuttall, S.D.4
  • 40
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-β spines reveal varied steric zippers
    • PMID:17468747
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, et al. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 2007; 447:453-7; PMID:17468747; http://dx.doi.org/10.1038/ nature05695.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5    Apostol, M.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.