Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 649

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

Cao, Yiping, Mezzenga, Raffaele·2019·Advances in Colloid and Interface Science
DOI 10.1016/j.cis.2019.05.002
Open this paper in CoChat — free account

Abstract

Amyloid fibrils have traditionally been considered only as pathological aggregates in human neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form amyloid fibrils is a generic property for all proteins, including food proteins. Differently from the pathological amyloid fibrils, those derived from food proteins can be used as advanced materials in biomedicine, tissue engineering, environmental science, nanotechnology, material science as well as in food science, owing to a combination of highly desirable feature such as extreme aspect ratios, outstanding stiffness and a broad availability of functional groups on their surfaces. In food science, protein fibrillization is progressively recognized as an appealing strategy to broaden and improve food protein functionality. This review article discusses the various classes of reported food protein amyloid fibrils and their formation conditions. It furthermore considers amyloid fibrils in a broad context, from their structural characterization to their forming mechanisms and ensued physical properties, emphasizing their applications in food-related fields. Finally, the biological fate and the potential toxicity mechanisms of food amyloid fibrils are discussed, and an experimental protocol for their health safety validation is proposed in the concluding part of the review.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.cis.2019.05.002

Cites

9 of 9 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 9 references

Research works printed but not linked: 283

  1. Mine, 1995, Recent advances in the understanding of egg-white protein functionality, Trends Food Sci Technol, 6, 225, 10.1016/S0924-2244(00)89083-4 · DOI · Paper page
  2. Foegeding, 2002, Advances in modifying and understanding whey protein functionality, Trends Food Sci Technol, 13, 151, 10.1016/S0924-2244(02)00111-5 · DOI
  3. Moure, 2006, Functionality of oilseed protein products: a review, Food Res Int, 39, 945, 10.1016/j.foodres.2006.07.002 · DOI · Paper page
  4. Jansens, 2019, Rational design of amyloid-like fibrillary structures for tailoring food protein techno-functionality and their potential health implications, Compr Rev Food Sci F, 18, 84, 10.1111/1541-4337.12404 · DOI
  5. Young, 1994, Plant-proteins in relation to human protein and amino-acid nutrition, Am J Clin Nutr, 59, 1203s, 10.1093/ajcn/59.5.1203S · DOI · Paper page
  6. van Huis, 2013, Potential of insects as food and feed in assuring food security, Annu Rev Entomol, 58, 563, 10.1146/annurev-ento-120811-153704 · DOI
  7. Yi, 2013, Extraction and characterisation of protein fractions from five insect species, Food Chem, 141, 3341, 10.1016/j.foodchem.2013.05.115 · DOI · Paper page
  8. Panyam, 1996, Enhancing the functionality of food proteins by enzymatic modification, Trends Food Sci Technol, 7, 120, 10.1016/0924-2244(96)10012-1 · DOI
  9. Nicolai, 2013, Controlled food protein aggregation for new functionality, Curr Opin Colloid In, 18, 249, 10.1016/j.cocis.2013.03.001 · DOI · Paper page
  10. Tavano, 2013, Protein hydrolysis using proteases: an important tool for food biotechnology, J Mol Catal B-Enzym, 90, 1, 10.1016/j.molcatb.2013.01.011 · DOI · Paper page
  11. Kroes-Nijboer, 2012, Fibrillar structures in food, Food Funct, 3, 221, 10.1039/C1FO10163C · DOI
  12. Mohammadian, 2018, Technological functionality and biological properties of food protein nanofibrils formed by heating at acidic condition, Trends Food Sci Technol, 75, 115, 10.1016/j.tifs.2018.03.013 · DOI
  13. Sipe, 2000, History of the amyloid fibril, J Struct Biol, 130, 88, 10.1006/jsbi.2000.4221 · DOI · Paper page
  14. Chiti, 2006, Protein misfolding, functional amyloid, and human disease, Annu Rev Biochem, 75, 333, 10.1146/annurev.biochem.75.101304.123901 · DOI · Paper page
  15. Eisenberg, 2012, The amyloid state of proteins in human diseases, Cell, 148, 1188, 10.1016/j.cell.2012.02.022 · DOI · Paper page
  16. Knowles, 2010, Nanostructured films from hierarchical self-assembly of amyloidogenic proteins, Nat Nanotechnol, 5, 204, 10.1038/nnano.2010.26 · DOI · Paper page
  17. Watt, 2013, PMEL: a pigment cell-specific model for functional amyloid formation, Pigm Cell Melanoma R, 26, 300, 10.1111/pcmr.12067 · DOI
  18. Aymard, 1999, Static and dynamic scattering of beta-lactoglobulin aggregates formed after heat-induced denaturation at pH 2, Macromolecules, 32, 2542, 10.1021/ma981689j · DOI
  19. Kavanagh, 2000, Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels, Int J Biol Macromol, 28, 41, 10.1016/S0141-8130(00)00144-6 · DOI
  20. Veerman, 2003, Irreversible self-assembly of ovalbumin into fibrils and the resulting network rheology, Int J Biol Macromol, 33, 121, 10.1016/S0141-8130(03)00076-X · DOI
  21. Sagis, 2004, Mesoscopic properties of semiflexible amyloid fibrils, Langmuir, 20, 924, 10.1021/la035390s · DOI
  22. Akkermans, 2007, Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate, J Agric Food Chem, 55, 9877, 10.1021/jf0718897 · DOI
  23. Wei, 2017, Self–assembling peptide and protein amyloids: from structure to tailored function in nanotechnology, Chem Soc Rev, 46, 4661, 10.1039/C6CS00542J · DOI · Paper page
  24. Knowles, 2016, Amyloid fibrils as building blocks for natural and artificial functional materials, Adv Mater, 28, 6546, 10.1002/adma.201505961 · DOI · Paper page
  25. Li, 2012, Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties, Nat Nanotechnol, 7, 421, 10.1038/nnano.2012.62 · DOI · Paper page
  26. Bolisetty, 2016, Amyloid-carbon hybrid membranes for universal water purification, Nat Nanotechnol, 11, 365, 10.1038/nnano.2015.310 · DOI · Paper page
  27. Shen, 2017, Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron, Nat Nanotechnol, 12, 642, 10.1038/nnano.2017.58 · DOI · Paper page
  28. Bolisetty, 2019, Sustainable technologies for water purification from heavy metals: review and analysis, Chem Soc Rev, 48, 463, 10.1039/C8CS00493E · DOI · Paper page
  29. Veerman, 2003, A new multistep Ca2+-induced cold gelation process for beta-lactoglobulin, J Agric Food Chem, 51, 3880, 10.1021/jf0261396 · DOI
  30. Mohammadian, 2016, Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution, Food Hydrocoll, 52, 221, 10.1016/j.foodhyd.2015.06.022 · DOI
  31. Hu, 2018, Polyphenol-binding amyloid fibrils self-assemble into reversible hydrogels with antibacterial activity, ACS Nano, 12, 3385, 10.1021/acsnano.7b08969 · DOI · Paper page
  32. Hoyer, 2002, Dependence of alpha-synuclein aggregate morphology on solution conditions, J Mol Biol, 322, 383, 10.1016/S0022-2836(02)00775-1 · DOI · Paper page
  33. Pedersen, 2006, The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting, J Mol Biol, 355, 501, 10.1016/j.jmb.2005.09.100 · DOI
  34. Jimenez, 2002, The protofilament structure of insulin amyloid fibrils, Proc Natl Acad Sci USA, 99, 9196, 10.1073/pnas.142459399 · DOI · Paper page
  35. Pedersen, 2010, Amyloid structure - one but not the same: the many levels of fibrillar polymorphism, FEBS J, 277, 4591, 10.1111/j.1742-4658.2010.07888.x · DOI
  36. Meinhardt, 2009, A beta(1–40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils, J Mol Biol, 386, 869, 10.1016/j.jmb.2008.11.005 · DOI · Paper page
  37. Schmidt, 2009, Comparison of alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures, Proc Natl Acad Sci USA, 106, 19813, 10.1073/pnas.0905007106 · DOI
  38. Pauling, 1951, Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets, Proc Natl Acad Sci USA, 37, 729, 10.1073/pnas.37.11.729 · DOI · Paper page
  39. Sawaya, 2007, Atomic structures of amyloid cross-beta spines reveal varied steric zippers, Nature, 447, 453, 10.1038/nature05695 · DOI · Paper page
  40. Riek, 2016, The activities of amyloids from a structural perspective, Nature, 539, 227, 10.1038/nature20416 · DOI · Paper page
  41. Luo, 2018, Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation, Nat Struct Mol Biol, 25, 341, 10.1038/s41594-018-0050-8 · DOI
  42. Sunde, 1997, Common core structure of amyloid fibrils by synchrotron x-ray diffraction, J Mol Biol, 273, 729, 10.1006/jmbi.1997.1348 · DOI · Paper page
  43. Eisenberg, 2017, Structural studies of amyloid proteins at the molecular level, Annu Rev Biochem, 86, 69, 10.1146/annurev-biochem-061516-045104 · DOI
  44. Walti, 2016, Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril, Proc Natl Acad Sci USA, 113, E4976, 10.1073/pnas.1600749113 · DOI · Paper page
  45. Gremer, 2017, Fibril structure of amyloid-beta(1–42) by cryo-electron microscopy, Science, 358, 116, 10.1126/science.aao2825 · DOI · Paper page
  46. Adamcik, 2010, Understanding amyloid aggregation by statistical analysis of atomic force microscopy images, Nat Nanotechnol, 5, 423, 10.1038/nnano.2010.59 · DOI · Paper page
  47. Adamcik, 2018, Amyloid polymorphism in the protein folding and aggregation energy landscape, Angew Chem Int Ed, 57, 8370, 10.1002/anie.201713416 · DOI · Paper page
  48. Lara, 2011, General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons, Biomacromolecules, 12, 1868, 10.1021/bm200216u · DOI
  49. Xiao, 2015, A beta(1–42) fibril structure illuminates self-recognition and replication of amyloid in alzheimer's disease, Nat Struct Mol Biol, 22, 499, 10.1038/nsmb.2991 · DOI · Paper page
  50. Colvin, 2016, Atomic resolution structure of monomorphic Aβ(42) amyloid fibrils, J Am Chem Soc, 138, 9663, 10.1021/jacs.6b05129 · DOI · Paper page
  51. Wiltzius, 2009, Molecular mechanisms for protein-encoded inheritance, Nat Struct Mol Biol, 16, 973, 10.1038/nsmb.1643 · DOI · Paper page
  52. Reynolds, 2017, Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides, Nat Commun, 8, 1338, 10.1038/s41467-017-01424-4 · DOI
  53. Balbirnie, 2001, An amyloid-forming peptide from the yeast prion sup35 reveals a dehydrated beta-sheet structure for amyloid, Proc Natl Acad Sci USA, 98, 2375, 10.1073/pnas.041617698 · DOI · Paper page
  54. Hirota-Nakaoka, 2003, Dissolution of beta(2)-microglobulin amyloid fibrils by dimethylsulfoxide, J Biochem, 134, 159, 10.1093/jb/mvg124 · DOI
  55. Nelson, 2005, Structure of the cross-beta spine of amyloid-like fibrils, Nature, 435, 773, 10.1038/nature03680 · DOI · Paper page
  56. Tsemekhman, 2007, Cooperative hydrogen bonding in amyloid formation, Protein Sci, 16, 761, 10.1110/ps.062609607 · DOI
  57. Murray, 2017, Structure of fus protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains, Cell, 171, 615, 10.1016/j.cell.2017.08.048 · DOI · Paper page
  58. Biancalana, 2010, Molecular mechanism of thioflavin-t binding to amyloid fibrils, Bba-Proteins Proteom, 1804, 1405, 10.1016/j.bbapap.2010.04.001 · DOI · Paper page
  59. Westermark, 1999, Staining methods for identification of amyloid in tissue, Methods Enzymol, 309, 3, 10.1016/S0076-6879(99)09003-5 · DOI · Paper page
  60. Stathopulos, 2004, Sonication of proteins causes formation of aggregates that resemble amyloid, Protein Sci, 13, 3017, 10.1110/ps.04831804 · DOI · Paper page
  61. Klunk, 1999, Quantifying amyloid by congo red spectral shift assay, Methods Enzymol, 309, 285, 10.1016/S0076-6879(99)09021-7 · DOI
  62. Bolognesi, 2010, Ans binding reveals common features of cytotoxic amyloid species, ACS Chem Biol, 5, 735, 10.1021/cb1001203 · DOI · Paper page
  63. Younan, 2015, A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies. ThT (thioflavin t); ANS (1-anilinonaphthalene-8-sulfonic acid); and bisANS (4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid), Biochemistry-Us, 54, 4297, 10.1021/acs.biochem.5b00309 · DOI
  64. Micsonai, 2015, Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy, Proc Natl Acad Sci USA, 112, E3095, 10.1073/pnas.1500851112 · DOI · Paper page
  65. Schierle, 2011, In situ measurements of the formation and morphology of intracellular beta-amyloid fibrils by super-resolution fluorescence imaging, J Am Chem Soc, 133, 12902, 10.1021/ja201651w · DOI
  66. Pinotsi, 2014, Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy, Nano Lett, 14, 339, 10.1021/nl4041093 · DOI
  67. Jung, 2008, Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate, Biomacromolecules, 9, 2477, 10.1021/bm800502j · DOI · Paper page
  68. Bolisetty, 2012, Gelation, phase behavior, and dynamics of beta-lactoglobulin amyloid fibrils at varying concentrations and ionic strengths, Biomacromolecules, 13, 3241, 10.1021/bm301005w · DOI
  69. Petkova, 2002, A structural model for alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR, Proc Natl Acad Sci USA, 99, 16742, 10.1073/pnas.262663499 · DOI · Paper page
  70. Heise, 2005, Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR, Proc Natl Acad Sci USA, 102, 15871, 10.1073/pnas.0506109102 · DOI · Paper page
  71. Tycko, 2011, Solid-state NMR studies of amyloid fibril structure, Annu Rev Phys Chem, 62, 279, 10.1146/annurev-physchem-032210-103539 · DOI
  72. Adamcik, 2011, Single-step direct measurement of amyloid fibrils stiffness by peak force quantitative nanomechanical atomic force microscopy, Appl Phys Lett, 98, 193701, 10.1063/1.3589369 · DOI
  73. Lara, 2012, Self-assembly of ovalbumin into amyloid and non-amyloid fibrils, Biomacromolecules, 13, 4213, 10.1021/bm301481v · DOI
  74. Akkermans, 2008, Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2, Biomacromolecules, 9, 1474, 10.1021/bm7014224 · DOI · Paper page
  75. Bateman, 2010, In vitro digestion of beta-lactoglobulin fibrils formed by heat treatment at low pH, J Agric Food Chem, 58, 9800, 10.1021/jf101722t · DOI
  76. Kavanagh, 2000, Heat-induced gelation of globular proteins: 4. Gelation kinetics of low ph beta-lactoglobulin gels, Langmuir, 16, 9584, 10.1021/la0004698 · DOI
  77. Loveday, 2012, Whey protein nanofibrils: kinetic, rheological and morphological effects of group IA and IIA cations, Int Dairy J, 26, 133, 10.1016/j.idairyj.2012.03.001 · DOI
  78. Gosal, 2002, Novel amyloid fibrillar networks derived from a globular protein: beta-lactoglobulin, Langmuir, 18, 7174, 10.1021/la025531a · DOI
  79. Arnaudov, 2003, Multiple steps during the formation of beta-lactoglobulin fibrils, Biomacromolecules, 4, 1614, 10.1021/bm034096b · DOI
  80. Bolisetty, 2011, Snapshots of fibrillation and aggregation kinetics in multistranded amyloid beta-lactoglobulin fibrils, Soft Matter, 7, 493, 10.1039/C0SM00502A · DOI
  81. Kotarek, 2008, Quartz crystal microbalance analysis of growth kinetics for aggregation intermediates of the amyloid-beta protein, Anal Biochem, 378, 15, 10.1016/j.ab.2008.03.022 · DOI
  82. Knowles, 2007, Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass, Proc Natl Acad Sci USA, 104, 10016, 10.1073/pnas.0610659104 · DOI
  83. Kumar, 2018, Detection of amyloid fibrils in Parkinson's disease using plasmonic chirality, Proc Natl Acad Sci USA, 115, 3225, 10.1073/pnas.1721690115 · DOI · Paper page
  84. Chiti, 2017, Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade, Annu Rev Biochem, 86, 27, 10.1146/annurev-biochem-061516-045115 · DOI · Paper page
  85. Balchin, 2016, In vivo aspects of protein folding and quality control, Science, 353, aac4354, 10.1126/science.aac4354 · DOI · Paper page
  86. Guijarro, 1998, Amyloid fibril formation by an SH3 domain, Proc Natl Acad Sci USA, 95, 4224, 10.1073/pnas.95.8.4224 · DOI · Paper page
  87. Fandrich, 2001, Amyloid fibrils from muscle myoglobin - even an ordinary globular protein can assume a rogue guise if conditions are right, Nature, 410, 165
  88. Konno, 1999, Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin, FEBS Lett, 454, 122, 10.1016/S0014-5793(99)00789-9 · DOI
  89. Goldschmidt, 2010, Identifying the amylome, proteins capable of forming amyloid-like fibrils, Proc Natl Acad Sci USA, 107, 3487, 10.1073/pnas.0915166107 · DOI · Paper page
  90. Mezzenga, 2013, The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions, Rep Prog Phys, 76, 046601, 10.1088/0034-4885/76/4/046601 · DOI
  91. Gsponer, 2006, Theoretical approaches to protein aggregation, Protein Pept Lett, 13, 287, 10.2174/092986606775338407 · DOI
  92. Stefani, 2008, Protein folding and misfolding on surfaces, Int J Mol Sci, 9, 2515, 10.3390/ijms9122515 · DOI
  93. Loveday, 2019, Food proteins: technological, nutritional, and sustainability attributes of traditional and emerging proteins, Annu Rev Food Sci Technol, 10, 311, 10.1146/annurev-food-032818-121128 · DOI · Paper page
  94. Shewry, 2002, Cereal seed storage proteins: structures, properties and role in grain utilization, J Exp Bot, 53, 947, 10.1093/jexbot/53.370.947 · DOI · Paper page
  95. Uversky, 2008, Amyloidogenesis of natively unfolded proteins, Curr Alzheimer Res, 5, 260, 10.2174/156720508784533312 · DOI
  96. van der Linden, 2007, Self-assembly and aggregation of proteins, Curr Opin Colloid In, 12, 158, 10.1016/j.cocis.2007.07.010 · DOI
  97. Loveday, 2011, Effect of pH, NaCl, CaCl2 and temperature on self-assembly of beta-lactoglobulin into nanofibrils: a central composite design study, J Agric Food Chem, 59, 8467, 10.1021/jf201870z · DOI
  98. Serfert, 2014, Characterisation and use of beta-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof, J Food Eng, 143, 53, 10.1016/j.jfoodeng.2014.06.026 · DOI
  99. Schmitt, 2009, Multiscale characterization of individualized beta-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions, Langmuir, 25, 7899, 10.1021/la900501n · DOI
  100. Dobson, 1999, Protein misfolding, evolution and disease, Trends Biochem Sci, 24, 329, 10.1016/S0968-0004(99)01445-0 · DOI
  101. Loveday, 2017, Beta-lactoglobulin nanofibrils: the long and the short of it, Int Dairy J, 67, 35, 10.1016/j.idairyj.2016.09.011 · DOI
  102. Gosal, 2004, Fibrillar beta-lactoglobulin gels: part 1. Fibril formation and structure, Biomacromolecules, 5, 2408, 10.1021/bm049659d · DOI
  103. Hamada, 2002, A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea, Protein Sci, 11, 2417, 10.1110/ps.0217702 · DOI · Paper page
  104. Lasse, 2016, Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white, Food Chem, 192, 491, 10.1016/j.foodchem.2015.07.044 · DOI
  105. Loveday, 2010, Tuning the properties of beta-lactoglobulin nanofibrils with pH, NaCl and CaCl2, Int Dairy J, 20, 571, 10.1016/j.idairyj.2010.02.014 · DOI
  106. Loveday, 2012, Beta-lactoglobulin nanofibrils: effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions, Food Hydrocoll, 27, 242, 10.1016/j.foodhyd.2011.07.001 · DOI
  107. Loveday, 2016, Beta-lactoglobulin heat denaturation: a critical assessment of kinetic modelling, Int Dairy J, 52, 92, 10.1016/j.idairyj.2015.08.001 · DOI
  108. Bolder, 2007, Effect of stirring and seeding on whey protein fibril formation, J Agric Food Chem, 55, 5661, 10.1021/jf063351r · DOI
  109. Bolder, 2007, Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation, Int Dairy J, 17, 846, 10.1016/j.idairyj.2006.10.002 · DOI
  110. Akkermans, 2008, Enzyme-induced formation of beta-lactoglobulin fibrils by AspN endoproteinase, Food Biophys, 3, 390, 10.1007/s11483-008-9094-3 · DOI
  111. Gao, 2013, The effect of limited proteolysis by different proteases on the formation of whey protein fibrils, J Dairy Sci, 96, 7383, 10.3168/jds.2013-6843 · DOI
  112. Hill, 2006, Shear flow induces amyloid fibril formation, Biomacromolecules, 7, 10, 10.1021/bm0505078 · DOI
  113. Dunstan, 2009, Shear-induced structure and mechanics of beta-lactoglobulin amyloid fibrils, Soft Matter, 5, 5020, 10.1039/b914089a · DOI
  114. Sharma, 2014, Effects of a flow field on amyloid fibrillogenesis in a beta-lactoglobulin solution, Int J Biol Macromol, 70, 490, 10.1016/j.ijbiomac.2014.06.034 · DOI
  115. Hettiarachchi, 2012, Formation of beta-lactoglobulin nanofibrils by microwave heating gives a peptide composition different from conventional heating, Biomacromolecules, 13, 2868, 10.1021/bm300896r · DOI
  116. Zappone, 2013, Catalytic activity of copper ions in the amyloid fibrillation of beta-lactoglobulin, Soft Matter, 9, 2412, 10.1039/c2sm27408f · DOI
  117. Guzzi, 2015, Ferric ions inhibit the amyloid fibrillation of beta-lactoglobulin at high temperature, Biomacromolecules, 16, 1794, 10.1021/acs.biomac.5b00371 · DOI
  118. Rasmussen, 2007, Formation of structured polymers upon controlled denaturation of beta-lactoglobulin with different chaotropes, Biopolymers, 86, 57, 10.1002/bip.20704 · DOI
  119. Goers, 2002, Conformational prerequisites for alpha-lactalbumin fibrillation, Biochemistry-Us, 41, 12546, 10.1021/bi0262698 · DOI
  120. Wang, 2011, Fibril formation of bovine alpha-lactalbumin is inhibited by glutathione, Food Biophys, 6, 138, 10.1007/s11483-010-9199-3 · DOI
  121. Yang, 2006, Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH, J Mol Biol, 362, 821, 10.1016/j.jmb.2006.07.059 · DOI
  122. Ipsen, 2001, Molecular self-assembly of partially hydrolysed alpha-lactalbumin resulting in strong gels with a novel microstructure, J Dairy Res, 68, 277, 10.1017/S0022029901004769 · DOI
  123. Graveland-Bikker, 2004, Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin, Langmuir, 20, 6841, 10.1021/la049579v · DOI
  124. Otte, 2005, Formation of amyloid-like fibrils upon limited proteolysis of bovine alpha-lactalbumin, Int Dairy J, 15, 219, 10.1016/j.idairyj.2004.07.004 · DOI
  125. Graveland-Bikker, 2006, Unique milk protein based nanotubes: food and nanotechnology meet, Trends Food Sci Technol, 17, 196, 10.1016/j.tifs.2005.12.009 · DOI · Paper page
  126. Ipsen, 2007, Self-assembly of partially hydrolysed alpha-lactalbumin, Biotechnol Adv, 25, 602, 10.1016/j.biotechadv.2007.07.006 · DOI
  127. Geng, 2016, Formation of nanotubes and gels at a broad ph range upon partial hydrolysis of bovine alpha-lactalbumin, Int Dairy J, 52, 72, 10.1016/j.idairyj.2015.08.005 · DOI
  128. Knowles, 2007, Role of intermolecular forces in defining material properties of protein nanofibrils, Science, 318, 1900, 10.1126/science.1150057 · DOI · Paper page
  129. Ghahghaei, 2010, The effects of molecular crowding on the amyloid fibril formation of alpha-lactalbumin and the chaperone action of alpha-casein, Protein J, 29, 257, 10.1007/s10930-010-9247-3 · DOI
  130. Thorn, 2008, Amyloid fibril formation by bovine milk alpha(s2)-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha(s1)-casein, Biochemistry-Us, 47, 3926, 10.1021/bi701278c · DOI
  131. Thorn, 2005, Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alpha(s-) and beta-casein, Biochemistry-Us, 44, 17027, 10.1021/bi051352r · DOI
  132. Koudelka, 2012, Methionine oxidation enhances kappa-casein amyloid fibril formation, J Agric Food Chem, 60, 4144, 10.1021/jf205168t · DOI
  133. Farrell, 2003, Environmental influences on bovine kappa-casein: reduction and conversion to fibrillar (amyloid) structures, J Protein Chem, 22, 259, 10.1023/A:1025020503769 · DOI
  134. Liu, 2016, The effect of milk constituents and crowding agents on amyloid fibril formation by kappa-casein, J Agric Food Chem, 64, 1335, 10.1021/acs.jafc.5b04977 · DOI
  135. Dalpadado, 2016, Real-time monitoring of amyloid growth in a rigid gel matrix, Anal Biochem, 511, 13, 10.1016/j.ab.2016.07.024 · DOI
  136. Pan, 2015, Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties, Soft Matter, 11, 5898, 10.1039/C5SM01037C · DOI
  137. Pearce, 2007, Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing, J Agric Food Chem, 55, 318, 10.1021/jf062154p · DOI
  138. Koseki, 1989, Irreversible thermal denaturation and formation of linear aggregates of ovalbumin, Food Hydrocoll, 3, 123, 10.1016/S0268-005X(89)80022-0 · DOI
  139. Kalapothakis, 2015, A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining, Biophys J, 108, 2300, 10.1016/j.bpj.2015.03.021 · DOI
  140. Naeem, 2011, A partially folded state of ovalbumin at low pH tends to aggregate, Cell Biochem Biophys, 59, 29, 10.1007/s12013-010-9108-x · DOI
  141. Arnaudov, 2005, Thermally induced fibrillar aggregation of hen egg white lysozyme, Biophys J, 88, 515, 10.1529/biophysj.104.048819 · DOI · Paper page
  142. Lara, 2013, Towards lysozyme nanotube and 3D hybrid self-assembly, Nanoscale, 5, 7197, 10.1039/c3nr02194g · DOI
  143. Krebs, 2000, Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain, J Mol Biol, 300, 541, 10.1006/jmbi.2000.3862 · DOI · Paper page
  144. Frare, 2004, A highly amyloidogenic region of hen lysozyme, J Mol Biol, 340, 1153, 10.1016/j.jmb.2004.05.056 · DOI · Paper page
  145. Mishra, 2007, Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion, J Mol Biol, 366, 1029, 10.1016/j.jmb.2006.11.084 · DOI
  146. Goda, 2000, Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution, Protein Sci, 9, 369, 10.1110/ps.9.2.369 · DOI
  147. Holley, 2008, Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution, Biochem Bioph Res Co, 373, 164, 10.1016/j.bbrc.2008.06.018 · DOI
  148. Yonezawa, 2002, An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle x-ray and neutron scattering study, J Mol Biol, 323, 237, 10.1016/S0022-2836(02)00941-5 · DOI
  149. Vernaglia, 2004, Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme, Biomacromolecules, 5, 1362, 10.1021/bm0498979 · DOI
  150. Cao, 2004, Formation of amyloid fibrils from fully reduced hen egg white lysozyme, Protein Sci, 13, 319, 10.1110/ps.03183404 · DOI
  151. Humblet-Hua, 2008, Effects of flow on hen egg white lysozyme (HEWL) fibril formation: length distribution, flexibility, and kinetics, J Agric Food Chem, 56, 11875, 10.1021/jf803377n · DOI
  152. Wei, 2019, Assembly of iron-bound ovotransferrin amyloid fibrils, Food Hydrocoll, 89, 579, 10.1016/j.foodhyd.2018.11.028 · DOI
  153. Jurado, 2019, Apoferritin protein amyloid fibrils with tunable chirality and polymorphism, J Am Chem Soc, 141, 1606, 10.1021/jacs.8b11418 · DOI
  154. Usov, 2013, Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils, ACS Nano, 7, 10465, 10.1021/nn404886k · DOI
  155. Veerman, 2003, Mesostructure of fibrillar bovine serum albumin gels, Int J Biol Macromol, 31, 139, 10.1016/S0141-8130(02)00074-0 · DOI
  156. Bhattacharya, 2011, Insights into the mechanism of aggregation and fibril formation from bovine serum albumin, J Phys Chem B, 115, 4195, 10.1021/jp111528c · DOI
  157. Holm, 2007, Aggregation and fibrillation of bovine serum albumin, Bba-Proteins Proteom, 1774, 1128, 10.1016/j.bbapap.2007.06.008 · DOI · Paper page
  158. Vetri, 2011, Bovine serum albumin protofibril-like aggregates formation: solo but not simple mechanism, Arch Biochem Biophys, 508, 13, 10.1016/j.abb.2011.01.024 · DOI
  159. Jayawardena, 2017, Amyloid fibrils from hemoglobin, Biomolecules, 7, 37, 10.3390/biom7020037 · DOI
  160. An, 2016, Hydrophobicity-modulating self-assembled morphologies of alpha-zein in aqueous ethanol, Int J Food Sci Tech, 51, 2621, 10.1111/ijfs.13248 · DOI
  161. Zhang, 2014, Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels, Food Sci Biotechnol, 23, 1417, 10.1007/s10068-014-0194-1 · DOI
  162. Huang, 2014, Self-assembly of rice bran globulin fibrils in electrostatic screening: nanostructure and gels, J Nanomater, 2014, 114, 10.1155/2014/951240 · DOI
  163. Ridgley, 2013, Evolution of the amyloid fiber over multiple length scales, ACS Nano, 7, 1006, 10.1021/nn303489a · DOI
  164. Athamneh, 2009, Enzyme-mediated self-assembly of highly ordered structures from disordered proteins, Smart Mater Struct, 18, 104024, 10.1088/0964-1726/18/10/104024 · DOI
  165. Mackintosh, 2009, Wheat glutenin proteins assemble into a nanostructure with unusual structural features, J Cereal Sci, 49, 157, 10.1016/j.jcs.2008.08.003 · DOI
  166. Ridgley, 2012, The effect of processing on large, self-assembled amyloid fibers, Soft Matter, 8, 10298, 10.1039/c2sm26496j · DOI
  167. Ridgley, 2014, The role of protein hydrophobicity in conformation change and self-assembly into large amyloid fibers, Biomacromolecules, 15, 1240, 10.1021/bm401815u · DOI
  168. Tang, 2010, Formation and characterization of amyloid-like fibrils from soy beta-conglycinin and glycinin, J Agric Food Chem, 58, 11058, 10.1021/jf1021658 · DOI
  169. Xia, 2017, Formation of amyloid fibrils from soy protein hydrolysate: effects of selective proteolysis on beta-conglycinin, Food Res Int, 100, 268, 10.1016/j.foodres.2017.08.059 · DOI
  170. Wan, 2016, Contribution of long fibrils and peptides to surface and foaming behavior of soy protein fibril system, Langmuir, 32, 8092, 10.1021/acs.langmuir.6b01511 · DOI
  171. Munialo, 2014, Fibril formation from pea protein and subsequent gel formation, J Agric Food Chem, 62, 2418, 10.1021/jf4055215 · DOI
  172. Liu, 2013, Heat-induced fibril assembly of vicilin at pH 2.0: reaction kinetics, influence of ionic strength and protein concentration, and molecular mechanism, Food Res Int, 51, 621, 10.1016/j.foodres.2012.12.049 · DOI
  173. Tang, 2010, Formation of amyloid fibrils from kidney bean 7S globulin (phaseolin) at pH 2.0, J Agric Food Chem, 58, 8061, 10.1021/jf101311f · DOI
  174. Zhou, 2014, Formation of heat-induced cottonseed congossypin(7S) fibrils at pH 2.0, J Sci Food Agr, 94, 2009, 10.1002/jsfa.6517 · DOI
  175. Kroes-Nijboer, 2011, Influence of protein hydrolysis on the growth kinetics of beta-lg fibrils, Langmuir, 27, 5753, 10.1021/la104797u · DOI
  176. Brown, 1992, Recent perspectives concerning the mechanism of H3O+-promoted and OH--promoted amide hydrolysis, Acc Chem Res, 25, 481, 10.1021/ar00023a001 · DOI
  177. Schultz, 1967, [28] cleavage at aspartic acid, vol. 11, 255, 10.1016/S0076-6879(67)11030-6 · DOI
  178. Adamcik, 2011, Adjustable twisting periodic pitch of amyloid fibrils, Soft Matter, 7, 5437, 10.1039/c1sm05382e · DOI
  179. vandenAkker, 2011, Morphology and persistence length of amyloid fibrils are correlated to peptide molecular structure, J Am Chem Soc, 133, 18030, 10.1021/ja206513r · DOI
  180. Kroes-Nijboer, 2009, The critical aggregation concentration of beta-lactoglobulin-based fibril formation, Food Biophys, 4, 59, 10.1007/s11483-009-9101-3 · DOI
  181. Petkova, 2005, Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils, Science, 307, 262, 10.1126/science.1105850 · DOI · Paper page
  182. Chatani, 2009, Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils, Proc Natl Acad Sci USA, 106, 11119, 10.1073/pnas.0901422106 · DOI
  183. Gross, 1994, Proteins under pressure - the influence of high hydrostatic-pressure on structure, function and assembly of proteins and protein complexes, Eur J Biochem, 221, 617, 10.1111/j.1432-1033.1994.tb18774.x · DOI · Paper page
  184. Mozhaev, 1996, High pressure effects on protein structure and function, Proteins, 24, 81, 10.1002/(SICI)1097-0134(199601)24:1<81::AID-PROT6>3.0.CO;2-R · DOI
  185. Vaneldik, 1989, Activation and reaction volumes in solution. 2, Chem Rev, 89, 549, 10.1021/cr00093a005 · DOI · Paper page
  186. Silva, 2001, Pressure provides new insights into protein folding, dynamics and structure, Trends Biochem Sci, 26, 612, 10.1016/S0968-0004(01)01949-1 · DOI · Paper page
  187. Silva, 1993, Pressure stability of proteins, Annu Rev Phys Chem, 44, 89, 10.1146/annurev.pc.44.100193.000513 · DOI · Paper page
  188. Torrent, 2004, High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation, Biochemistry-Us, 43, 7162, 10.1021/bi049939d · DOI
  189. Jansen, 2004, High pressure promotes circularly shaped insulin amyloid, J Mol Biol, 338, 203, 10.1016/j.jmb.2004.02.056 · DOI
  190. Foguel, 2003, Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities, Proc Natl Acad Sci USA, 100, 9831, 10.1073/pnas.1734009100 · DOI
  191. Mishra, 2008, Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils, Angew Chem Int Ed, 47, 6518, 10.1002/anie.200802027 · DOI
  192. Radovan, 2008, Effect of pressure on islet amyloid polypeptide aggregation: revealing the polymorphic nature of the fibrillation process, Biochemistry-Us, 47, 6352, 10.1021/bi800503j · DOI
  193. Shah, 2012, Pressure-accelerated dissociation of amyloid fibrils in wild-type hen lysozyme, Biophys J, 102, 121, 10.1016/j.bpj.2011.10.041 · DOI
  194. Dirix, 2005, High hydrostatic pressure dissociates early aggregates of TTR105–115, but not the mature amyloid fibrils, J Mol Biol, 347, 903, 10.1016/j.jmb.2005.01.073 · DOI
  195. Brandts, 1967, Thermodynamics of protein denaturation. Iii. Denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures, J Am Chem Soc, 89, 4826, 10.1021/ja00995a002 · DOI · Paper page
  196. Thomas, 1993, Local and nonlocal interactions in globular-proteins and mechanisms of alcohol denaturation, Protein Sci, 2, 2050, 10.1002/pro.5560021206 · DOI · Paper page
  197. Jordens, 2011, Disassembly and reassembly of amyloid fibrils in water-ethanol mixtures, Biomacromolecules, 12, 187, 10.1021/bm101119t · DOI
  198. Yang, 2015, Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin, J Phys Chem B, 119, 3969, 10.1021/acs.jpcb.5b00144 · DOI
  199. Veerman, 2002, Effect of electrostatic interactions on the percolation concentration of fibrillar beta-lactoglobulin gels, Biomacromolecules, 3, 869, 10.1021/bm025533+ · DOI
  200. Schokker, 2000, Heat-induced aggregation of beta-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration, Int Dairy J, 10, 233, 10.1016/S0958-6946(00)00047-9 · DOI

200 of 283 shown

Cited by

Metadata

Authors
Cao, Y., & Mezzenga, R.
Venue
Advances in Colloid and Interface Science
Publisher
Elsevier BV
Published
2019-07
Volume
269
Pages
334-356
ISSN
0001-8686 (ISSN-L)
DOI
10.1016/j.cis.2019.05.002
OpenAlex
W2943891617
Cited by
649
References
9
FWCI
30.10
Type
journal article
Language
en
Open access
closed
Licence
  • www.elsevier.com/tdm/userlicense/1.0/ (tdm)
  • www.elsevier.com/legal/tdmrep-license (tdm)
Funders
  • ETH Zurich
  • China Scholarship Council

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.