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Volumn 16, Issue 1, 2015, Pages 326-335

Stable, metastable, and kinetically trapped amyloid aggregate phases

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AGGREGATES; GLYCOPROTEINS; LIQUIDS; METASTABLE PHASES; NEURODEGENERATIVE DISEASES; OLIGOMERS; PHASE SEPARATION; SELF ASSEMBLY;

EID: 84921046821     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm501521r     Document Type: Article
Times cited : (79)

References (57)
  • 1
    • 0029981197 scopus 로고    scopus 로고
    • Alternative Conformations of Amyloidogenic Proteins Govern Their Behavior
    • Kelly, J. W. Alternative Conformations of Amyloidogenic Proteins Govern Their Behavior. Curr. Opin. Struct. Biol. 1996, 6, 11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 0033200063 scopus 로고    scopus 로고
    • Protein Misfolding, Evolution, and Disease
    • Dobson, C. M. Protein Misfolding, Evolution, and Disease. Trends Biochem. Sci. 1999, 24, 329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 4
    • 80053368232 scopus 로고    scopus 로고
    • Chain Collapse of an Amyloidogenic Intrinsically Disordered Protein
    • Jain, N.; Bhattacharya, M.; Mukhopadhyay, S. Chain Collapse of an Amyloidogenic Intrinsically Disordered Protein. Biophys. J. 2011, 101, 1720-1729.
    • (2011) Biophys. J. , vol.101 , pp. 1720-1729
    • Jain, N.1    Bhattacharya, M.2    Mukhopadhyay, S.3
  • 5
    • 0037126101 scopus 로고    scopus 로고
    • Novel Amyloid Fibrillar Networks Derived from a Globular Protein: β-Lactoglobulin
    • Gosal, W. S.; Clark, A. H.; Pudney, P. D. A.; Ross-Murphy, S. B. Novel Amyloid Fibrillar Networks Derived from a Globular Protein: β-Langmuir 2002, 18, 7174-7181.
    • (2002) Langmuir , vol.18 , pp. 7174-7181
    • Gosal, W.S.1    Clark, A.H.2    Pudney, P.D.A.3    Ross-Murphy, S.B.4
  • 7
    • 12344272183 scopus 로고    scopus 로고
    • Aggregation Across the Length-Scales in β-Lactoglobulin
    • Bromley, E. H. C.; Krebs, M. R. H.; Donald, A. M. Aggregation Across the Length-Scales in β-Lactoglobulin. Faraday Discuss. 2005, 128, 13-27.
    • (2005) Faraday Discuss. , vol.128 , pp. 13-27
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 9
    • 0034616839 scopus 로고    scopus 로고
    • Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly: Implications for Amyloid Fibril Formation and Materials Science
    • Lashuel, H. A.; LaBrenz, S. R.; Woo, L.; Serpell, L. C.; Kelly, J. W. Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly: Implications for Amyloid Fibril Formation and Materials Science. J. Am. Chem. Soc. 2000, 122, 5262-5277.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5262-5277
    • Lashuel, H.A.1    LaBrenz, S.R.2    Woo, L.3    Serpell, L.C.4    Kelly, J.W.5
  • 11
    • 0036845354 scopus 로고    scopus 로고
    • The Behavior of Polyamino Acids Reveals an Inverse Side Chain Effect in Amyloid Structure Formation
    • Fändrich, M.; Dobson, C. M. The Behavior of Polyamino Acids Reveals an Inverse Side Chain Effect in Amyloid Structure Formation. EMBO J. 2002, 21, 5682-5690.
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 12
    • 0030908095 scopus 로고    scopus 로고
    • Models of Amyloid Seeding in Alzheimer's Disease and Scrapie: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
    • Harper, J. D.; Lansbury, P. T. Models of Amyloid Seeding in Alzheimer's Disease and Scrapie: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins. Annu. Rev. Biochem. 1997, 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 13
    • 84863981137 scopus 로고    scopus 로고
    • From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
    • Cohen, S. I. A.; Vendruscolo, M.; Dobson, C. M.; Knowles, T. P. J. From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation. J. Mol. Biol. 2012, 421, 160-171.
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 14
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability
    • Dahlgren, K. N.; Manelli, A. M.; Stine, W. B.; Baker, J.; Lorinda, K.; Krafft, G. A.; LaDu, M. J. Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability. J. Biol. Chem. 2002, 277, 36046-36053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36046-36053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, J.4    Lorinda, K.5    Krafft, G.A.6    LaDu, M.J.7
  • 15
    • 0037041426 scopus 로고    scopus 로고
    • Naturally Secreted Oligomers of Amyloid-β Protein Potently Inhibit Hippocampal Long-Term Potentiation in Vivo
    • Walsh, D. M.; Klyubin, I.; Fadeeva, J. V.; Cullen, W. K.; Anwyl, R.; Wolfe, M. S.; Rowan, M. J.; Selkoe, D. J. Naturally Secreted Oligomers of Amyloid-β Protein Potently Inhibit Hippocampal Long-Term Potentiation in Vivo. Nature 2002, 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 19
    • 0035297712 scopus 로고    scopus 로고
    • Targeting Small Aβ Oligomers: The Solution to an Alzheimer's Disease Conundrum?
    • Klein, W. L.; Krafft, G. A.; Finch, C. E. Targeting Small Aβ Oligomers: The Solution to an Alzheimer's Disease Conundrum? Trends Neurosci. 2001, 24, 219-224.
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 20
    • 0038176528 scopus 로고    scopus 로고
    • In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis
    • Stine, W. B., Jr.; Dahlgren, K. N.; Krafft, G. A.; LaDu, M. J. In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis. J. Biol. Chem. 2003, 278, 11612-11622.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 21
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious Oligomerization of the Amyloidogenic Proteins
    • Uversky, V. N. Mysterious Oligomerization of the Amyloidogenic Proteins. FEBS J. 2010, 277, 2940-2953.
    • (2010) FEBS J. , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 23
    • 84876491523 scopus 로고    scopus 로고
    • Parallel β-Sheet Fibril and Antiparallel β-Sheet Oligomer: New Insights into Amyloid Formation of Hen Egg White Lysozyme under Heat and Acidic Condition from FTIR Spectroscopy
    • Zou, Y.; Li, Y.; Hao, W.; Hu, X.; Ma, G. Parallel β-Sheet Fibril and Antiparallel β-Sheet Oligomer: New Insights into Amyloid Formation of Hen Egg White Lysozyme under Heat and Acidic Condition from FTIR Spectroscopy. J. Phys. Chem. B 2013, 117, 4003-4013.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 4003-4013
    • Zou, Y.1    Li, Y.2    Hao, W.3    Hu, X.4    Ma, G.5
  • 26
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus Aggregation: Polypeptide Conformations on Competing Pathways
    • Jahn, T. R.; Radford, S. E. Folding versus Aggregation: Polypeptide Conformations on Competing Pathways. Arch. Biochem. Biophys. 2008, 469, 100-117.
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 27
    • 0037960271 scopus 로고    scopus 로고
    • Micelle Formation by a Fragment of Human Islet Amyloid Polypeptide
    • Rhoades, E.; Gafni, A. Micelle Formation by a Fragment of Human Islet Amyloid Polypeptide. Biophys. J. 2003, 84, 3480-3487.
    • (2003) Biophys. J. , vol.84 , pp. 3480-3487
    • Rhoades, E.1    Gafni, A.2
  • 28
    • 79953695682 scopus 로고    scopus 로고
    • Spatial Extent of Charge Repulsion Regulates Assembly Pathways for Lysozyme Amyloid Fibrils
    • Hill, S. E.; Miti, T.; Richmond, T.; Muschol, M. Spatial Extent of Charge Repulsion Regulates Assembly Pathways for Lysozyme Amyloid Fibrils. PLoS One 2011, 6, e18171.1-e18171.12.
    • (2011) PLoS One , vol.6 , pp. e18171.1-e18171.12
    • Hill, S.E.1    Miti, T.2    Richmond, T.3    Muschol, M.4
  • 30
    • 52649129277 scopus 로고    scopus 로고
    • Structure of Heat-Induced β-Lactoglobulin Aggregates and Their Complexes with Sodium-Dodecyl Sulfate
    • Jung, J.-M.; Savin, G.; Pouzot, M.; Schmitt, C.; Mezzenga, R. Structure of Heat-Induced β-Lactoglobulin Aggregates and Their Complexes with Sodium-Dodecyl Sulfate. Biomacromolecules 2008, 9, 2477-2486.
    • (2008) Biomacromolecules , vol.9 , pp. 2477-2486
    • Jung, J.-M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 31
    • 84867441784 scopus 로고    scopus 로고
    • Gelation, Phase Behavior, and Dynamics of β-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths
    • Bolisetty, S.; Harnau, L.; Jung, J.-M.; Mezzenga, R. Gelation, Phase Behavior, and Dynamics of β-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths. Biomacromolecules 2012, 13, 3241-3252.
    • (2012) Biomacromolecules , vol.13 , pp. 3241-3252
    • Bolisetty, S.1    Harnau, L.2    Jung, J.-M.3    Mezzenga, R.4
  • 32
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the Intermediates and Products of Amyloid Assembly
    • Kodali, R.; Wetzel, R. Polymorphism in the Intermediates and Products of Amyloid Assembly. Curr. Opin. Struct. Biol. 2007, 17, 48-57.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 34
    • 11244340520 scopus 로고    scopus 로고
    • Thermally Induced Fibrillar Aggregation of Hen Egg White Lysozyme
    • Arnaudov, L. N.; de Vries, R. Thermally Induced Fibrillar Aggregation of Hen Egg White Lysozyme. Biophys. J. 2005, 88, 515-526.
    • (2005) Biophys. J. , vol.88 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 35
    • 67650403403 scopus 로고    scopus 로고
    • Amyloid Protofibrils of Lysozyme Nucleate and Grow via Oligomer Fusion
    • Hill, S. E.; Robinson, J.; Matthews, G.; Muschol, M. Amyloid Protofibrils of Lysozyme Nucleate and Grow via Oligomer Fusion. Biophys. J. 2009, 96, 3781-3790.
    • (2009) Biophys. J. , vol.96 , pp. 3781-3790
    • Hill, S.E.1    Robinson, J.2    Matthews, G.3    Muschol, M.4
  • 36
    • 34547575469 scopus 로고    scopus 로고
    • Submicron Lysozyme Clusters Distort Kinetics of Crystal Nucleation in Supersaturated Lysozyme Solutions
    • Parmar, A. S.; Gottschall, P. E.; Muschol, M. Submicron Lysozyme Clusters Distort Kinetics of Crystal Nucleation in Supersaturated Lysozyme Solutions. Biophys. Chem. 2007, 129, 224-234.
    • (2007) Biophys. Chem. , vol.129 , pp. 224-234
    • Parmar, A.S.1    Gottschall, P.E.2    Muschol, M.3
  • 37
    • 77949801502 scopus 로고    scopus 로고
    • The Stabilities of Protein Crystals
    • Schmit, J. D.; Dill, K. A. The Stabilities of Protein Crystals. J. Phys. Chem. B 2010, 114, 4020-4027.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4020-4027
    • Schmit, J.D.1    Dill, K.A.2
  • 39
    • 80052426201 scopus 로고    scopus 로고
    • Electrostatics and Aggregation: How Charge Can Turn a Crystal into a Gel
    • Schmit, J. D.; Whitelam, S.; Dill, K. Electrostatics and Aggregation: How Charge Can Turn a Crystal into a Gel. J. Chem. Phys. 2011, 135, 085103/1-085103/6.
    • (2011) J. Chem. Phys. , vol.135 , pp. 085103/1-085103/6
    • Schmit, J.D.1    Whitelam, S.2    Dill, K.3
  • 41
    • 84921064612 scopus 로고
    • Serum and Urinary Lysozyme in Patients with Mastocytosis (Urticaria Pigmentosa), Systemic Scleroderma, and Psoriasis1
    • Sasaki, S.; Asboe-Hansen, G. Serum and Urinary Lysozyme in Patients with Mastocytosis (Urticaria Pigmentosa), Systemic Scleroderma, and Psoriasis1. J. Invest. Dermatol. 1967, 49, 302-305.
    • (1967) J. Invest. Dermatol. , vol.49 , pp. 302-305
    • Sasaki, S.1    Asboe-Hansen, G.2
  • 42
    • 0013967156 scopus 로고
    • Serum and Urinary Lysozyme (Muramidase) in Monocytic and Monomyelocytic Leukemia
    • Osserman, E. F.; Lawlor, D. P. Serum and Urinary Lysozyme (Muramidase) in Monocytic and Monomyelocytic Leukemia. J. Exp. Med. 1966, 124, 921-952.
    • (1966) J. Exp. Med. , vol.124 , pp. 921-952
    • Osserman, E.F.1    Lawlor, D.P.2
  • 44
    • 0035177019 scopus 로고    scopus 로고
    • Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
    • Chamberlain, A. K.; Receveur, V.; Spencer, A.; Redfield, C.; Dobson, C. M. Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy. Protein Sci. 2001, 10, 2525-2530.
    • (2001) Protein Sci. , vol.10 , pp. 2525-2530
    • Chamberlain, A.K.1    Receveur, V.2    Spencer, A.3    Redfield, C.4    Dobson, C.M.5
  • 45
    • 35148865232 scopus 로고    scopus 로고
    • On the Structural Definition of Amyloid Fibrils and Other Polypeptide Aggregates
    • Fändrich, M. On the Structural Definition of Amyloid Fibrils and Other Polypeptide Aggregates. Cell. Mol. Life Sci. 2007, 64, 2066-2078.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2066-2078
    • Fändrich, M.1
  • 46
    • 9344243513 scopus 로고    scopus 로고
    • FTIR Reveals Structural Differences between Native β-Sheet Proteins and Amyloid Fibrils
    • Zandomeneghi, G.; Krebs, M. R. H.; McCammon, M. G.; Fändrich, M. FTIR Reveals Structural Differences between Native β-Sheet Proteins and Amyloid Fibrils. Protein Sci. 2004, 13, 3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fändrich, M.4
  • 48
    • 84903289360 scopus 로고    scopus 로고
    • Amyloid Oligomers and Protofibrils, but Not Filaments, Self-Replicate from Native Lysozyme
    • Mulaj, M.; Foley, J.; Muschol, M. Amyloid Oligomers and Protofibrils, but Not Filaments, Self-Replicate from Native Lysozyme. J. Am. Chem. Soc. 2014, 136, 8947-8956.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8947-8956
    • Mulaj, M.1    Foley, J.2    Muschol, M.3
  • 49
    • 84880377094 scopus 로고    scopus 로고
    • Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation
    • Apostol, M. I.; Perry, K.; Surewicz, W. K. Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation. J. Am. Chem. Soc. 2013, 135, 10202-10205.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 10202-10205
    • Apostol, M.I.1    Perry, K.2    Surewicz, W.K.3
  • 50
    • 70349503652 scopus 로고    scopus 로고
    • Isotropic-Nematic Phase Transition in Amyloid Fibrilization
    • Lee, C. F. Isotropic-Nematic Phase Transition in Amyloid Fibrilization. Phys. Rev. E 2009, 80, 031902-031906.
    • (2009) Phys. Rev. E , vol.80 , pp. 031902-031906
    • Lee, C.F.1
  • 51
    • 78751685655 scopus 로고    scopus 로고
    • Why Do Amyloid Molecules Assemble into Oligomers and Fibrils
    • Schmit, J. D.; Gosh, K.; Dill, K. Why Do Amyloid Molecules Assemble into Oligomers and Fibrils. Biophys. J. 2011, 100, 450-458.
    • (2011) Biophys. J. , vol.100 , pp. 450-458
    • Schmit, J.D.1    Gosh, K.2    Dill, K.3
  • 52
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-Liquid Phase Separation in Supersaturated Lysozyme Solutions and Associated Precipitate Formation/Crystallization
    • Muschol, M.; Rosenberger, F. Liquid-Liquid Phase Separation in Supersaturated Lysozyme Solutions and Associated Precipitate Formation/Crystallization. J. Chem. Phys. 1997, 107, 1953-1962.
    • (1997) J. Chem. Phys. , vol.107 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 53
    • 36449000890 scopus 로고
    • Determination of Phase-Diagrams for the Hard-Core Attractive Yukawa System
    • Hagen, M. H. J.; Frenkel, D. Determination of Phase-Diagrams for the Hard-Core Attractive Yukawa System. J. Chem. Phys. 1994, 101, 4093-4097.
    • (1994) J. Chem. Phys. , vol.101 , pp. 4093-4097
    • Hagen, M.H.J.1    Frenkel, D.2
  • 55
    • 84865694928 scopus 로고    scopus 로고
    • Two-Step Nucleation of Amyloid Fibrils: Omnipresent or Not?
    • Auer, S.; Ricchiuto, P.; Kashchiev, D. Two-Step Nucleation of Amyloid Fibrils: Omnipresent or Not? J. Mol. Biol. 2012, 422, 723-730.
    • (2012) J. Mol. Biol. , vol.422 , pp. 723-730
    • Auer, S.1    Ricchiuto, P.2    Kashchiev, D.3
  • 56
    • 0037453427 scopus 로고    scopus 로고
    • On the Origins of Morphological Complexity in Block Copolymer Surfactants
    • Jain, S.; Bates, F. S. On the Origins of Morphological Complexity in Block Copolymer Surfactants. Science 2003, 300, 460-464.
    • (2003) Science , vol.300 , pp. 460-464
    • Jain, S.1    Bates, F.S.2
  • 57
    • 84877795952 scopus 로고    scopus 로고
    • Direct Observation of the Formation of Surfactant Micelles under Nonisothermal Conditions by Synchrotron SAXS
    • Jensen, G. V.; Lund, R.; Gummel, J.; Monkenbusch, M.; Narayanan, T.; Pedersen, J. S. Direct Observation of the Formation of Surfactant Micelles under Nonisothermal Conditions by Synchrotron SAXS. J. Am. Chem. Soc. 2013, 135, 7214-7222.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7214-7222
    • Jensen, G.V.1    Lund, R.2    Gummel, J.3    Monkenbusch, M.4    Narayanan, T.5    Pedersen, J.S.6


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