70. Stradner A, Sedgwick H, Cardinaux F et al (2004) Equilibrium cluster formation in
concentrated protein solutions and colloids. Nature 432(7016):492–495
71. Liu Y, Porcar L, Chen J (2011) Lyzosyme protein solution with an intermediate range order
structure. J Phys Chem B 115(22):7238–7247
72. Stradner A, Cardinaux F, Schurtenberger P et al (2006) A small angle scattering study on
equilibrium clusters in lysozyme solution. J Phys Chem B 110(42):21222–21231
73. Bolder SG, Hendrickx H, Sagis LMC et al (2006) Fibril assemblies in aqueous whey protein
mixtures. J Agric Food Chem 54:4229–4234
74. Krebs MRH, Domike KR, Donald AM (2009) Protein aggregation: more than just fibrils.
Biochem Soc Trans 37(9):682–686
75. Schmitt C, Bovay C, Vuilliomenet A-M et al (2009) Multiscale characterization of
individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH
range conditions. Langmuir 25:7899–7909
76. Trexler AJ, Nilsoon MR (2007) The formation of amyloid fibrils from proteins in the
lysozyme family. Curr Protein Pept Sci 8:537–557
77. Lomakin A, Chung DS, Benedek GB et al (1996) On the nucleation and growth of amyloid
α-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci
USA 93:1125–1129
78. Lomakin A, Teplow DB, Kirschner DA et al (1997) Kinetic theory of fibrillogenesis of
amyloid b-protein. Proc Natl Acad Sci USA 94:7942–7947
79. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease.
Annu Rev Biochem 75:333–366
80. Pellarin R, Guarnera E, Caflisch A (2007) Pathways and intermediates of amyloid fibril
formation. J Mol Biol 374:917–924
81. Arnaudov LN, de Vries R (2007) Theoretical modeling of the kinetics of fibrilar aggregation
of bovine beta-lactoglobulin at pH 2. J Chem Phys 126:145106
82. Bolder SG, Sagis LMC, Venema P et al (2007) Effect of Stirling and seeding on whey
proteı ´na fibril formation. J Agric Food Chem 55:5661–5669
83. Loveday SM, Wang XL, Rao MA et al (2012) β-Lactoglobulin nanofibrils: effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril
dispersions. Food Hydrocolloid 27:242–249
84. Farrell H, Cooke P, Wickham E et al (2003) Environmental influences on bovine κ-casein:
reduction and conversion to fibrillar (amyloid) structures. J Protein Chem 22:259–273
85. Akkermans C, Venema P, van der Goot AJ et al (2008) Peptides are building blocks of heatinduced fibrillar proteins aggregates of β-Lg formed at pH 2. Biomacromolecules
9:1474–1479
86. Kroes-Nijboer A, Venema P, Bouman J et al (2011) Influence of protein hydrolysis on the
growth kinetics of β-Lg fibrils. Langmuir 27:5753–5761
87. Hamada D, Tanaka T, Tartaglia GG et al (2009) Competition between folding, native-state
dimerisation and amyloid aggregation in β-lactoglobulin. J Mol Biol 386:878–890
88. Arnaudov LN, de Vries R, Ippel H et al (2003) Multiple steps during the formation of
beta-lactoglobulin fibrils. Macromolecules 4:1614–1622
89. Arnaudov LN, de Vries R (2006) Strong impact of ionic strength on the kinetics of fibrilar
aggregation of β-lactoglobulin. Biomacromolecules 7:3490–3498
90. Bromley EHC, Krebs MRH, Donald AM (2005) Aggregation across the length scales in
β-lactoglobulin. Faraday Discuss 128:13–27
91. Krebs MRH, Bromley EHC, Rogers SS et al (2005) The mechanism of amyloid spherulite
formation by bovine insulin. Biophys J 88:2013–2021
92. Domike KR, Hardin E, Armstead DN et al (2009) Investigating the inner structure of irregular
β-lactoglobulin spherulites. Eur Phys J E 29:173–182
93. Rogers SS, Krebs MRH, Bromley EHC, van der Linden E, Donald AM (2006) Optical
microscopy of growing insulin amyloid spherulites on surfaces in vitro. Biophys J
90:1043–1054
98
S. Bouhallab and T. Croguennec
concentrated protein solutions and colloids. Nature 432(7016):492–495
71. Liu Y, Porcar L, Chen J (2011) Lyzosyme protein solution with an intermediate range order
structure. J Phys Chem B 115(22):7238–7247
72. Stradner A, Cardinaux F, Schurtenberger P et al (2006) A small angle scattering study on
equilibrium clusters in lysozyme solution. J Phys Chem B 110(42):21222–21231
73. Bolder SG, Hendrickx H, Sagis LMC et al (2006) Fibril assemblies in aqueous whey protein
mixtures. J Agric Food Chem 54:4229–4234
74. Krebs MRH, Domike KR, Donald AM (2009) Protein aggregation: more than just fibrils.
Biochem Soc Trans 37(9):682–686
75. Schmitt C, Bovay C, Vuilliomenet A-M et al (2009) Multiscale characterization of
individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH
range conditions. Langmuir 25:7899–7909
76. Trexler AJ, Nilsoon MR (2007) The formation of amyloid fibrils from proteins in the
lysozyme family. Curr Protein Pept Sci 8:537–557
77. Lomakin A, Chung DS, Benedek GB et al (1996) On the nucleation and growth of amyloid
α-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci
USA 93:1125–1129
78. Lomakin A, Teplow DB, Kirschner DA et al (1997) Kinetic theory of fibrillogenesis of
amyloid b-protein. Proc Natl Acad Sci USA 94:7942–7947
79. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease.
Annu Rev Biochem 75:333–366
80. Pellarin R, Guarnera E, Caflisch A (2007) Pathways and intermediates of amyloid fibril
formation. J Mol Biol 374:917–924
81. Arnaudov LN, de Vries R (2007) Theoretical modeling of the kinetics of fibrilar aggregation
of bovine beta-lactoglobulin at pH 2. J Chem Phys 126:145106
82. Bolder SG, Sagis LMC, Venema P et al (2007) Effect of Stirling and seeding on whey
proteı ´na fibril formation. J Agric Food Chem 55:5661–5669
83. Loveday SM, Wang XL, Rao MA et al (2012) β-Lactoglobulin nanofibrils: effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril
dispersions. Food Hydrocolloid 27:242–249
84. Farrell H, Cooke P, Wickham E et al (2003) Environmental influences on bovine κ-casein:
reduction and conversion to fibrillar (amyloid) structures. J Protein Chem 22:259–273
85. Akkermans C, Venema P, van der Goot AJ et al (2008) Peptides are building blocks of heatinduced fibrillar proteins aggregates of β-Lg formed at pH 2. Biomacromolecules
9:1474–1479
86. Kroes-Nijboer A, Venema P, Bouman J et al (2011) Influence of protein hydrolysis on the
growth kinetics of β-Lg fibrils. Langmuir 27:5753–5761
87. Hamada D, Tanaka T, Tartaglia GG et al (2009) Competition between folding, native-state
dimerisation and amyloid aggregation in β-lactoglobulin. J Mol Biol 386:878–890
88. Arnaudov LN, de Vries R, Ippel H et al (2003) Multiple steps during the formation of
beta-lactoglobulin fibrils. Macromolecules 4:1614–1622
89. Arnaudov LN, de Vries R (2006) Strong impact of ionic strength on the kinetics of fibrilar
aggregation of β-lactoglobulin. Biomacromolecules 7:3490–3498
90. Bromley EHC, Krebs MRH, Donald AM (2005) Aggregation across the length scales in
β-lactoglobulin. Faraday Discuss 128:13–27
91. Krebs MRH, Bromley EHC, Rogers SS et al (2005) The mechanism of amyloid spherulite
formation by bovine insulin. Biophys J 88:2013–2021
92. Domike KR, Hardin E, Armstead DN et al (2009) Investigating the inner structure of irregular
β-lactoglobulin spherulites. Eur Phys J E 29:173–182
93. Rogers SS, Krebs MRH, Bromley EHC, van der Linden E, Donald AM (2006) Optical
microscopy of growing insulin amyloid spherulites on surfaces in vitro. Biophys J
90:1043–1054
98
S. Bouhallab and T. Croguennec