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
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.
Integrity signals
Registry
Cites
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.
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
A standardised static in vitro digestion method suitable for food – an international consensus
Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C., Carrière, F., Boutrou, R., Corredig, M., Dupont, D., et al. (2014) · Food Funct. · doi:10.1039/c3fo60702j · Cited by 5,824
Host-Bacterial Mutualism in the Human Intestine
Bäckhed, F., Ley, R. E., Sonnenburg, J. L., Peterson, D. A., & Gordon, J. I. (2005) · Science · doi:10.1126/science.1104816 · Cited by 5,277
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Nanoparticles as potential oral delivery systems of proteins and vaccines: A mechanistic approach
des Rieux, A., Fievez, V., Garinot, M., Schneider, Y.-J., & Préat, V. (2006) · Journal of Controlled Release · doi:10.1016/j.jconrel.2006.08.013 · Cited by 1,305
The Alzheimer's Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide
Soscia, S. J., Kirby, J. E., Washicosky, K. J., Tucker, S. M., Ingelsson, M., Hyman, B., Burton, M. A., Goldstein, L. E., Duong, S., Tanzi, R. E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009505 · Cited by 1,060
FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Food protein functionality: A comprehensive approach
Foegeding, E. A., & Davis, J. P. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.05.008 · Cited by 486
Phillips, G. O., & Williams, P. A. (2011) · doi:10.1533/9780857093639 · Cited by 256
Research works printed but not linked: 283
- 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
- Foegeding, 2002, Advances in modifying and understanding whey protein functionality, Trends Food Sci Technol, 13, 151, 10.1016/S0924-2244(02)00111-5 · DOI
- Moure, 2006, Functionality of oilseed protein products: a review, Food Res Int, 39, 945, 10.1016/j.foodres.2006.07.002 · DOI · Paper page
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Kroes-Nijboer, 2012, Fibrillar structures in food, Food Funct, 3, 221, 10.1039/C1FO10163C · DOI
- 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
- Sipe, 2000, History of the amyloid fibril, J Struct Biol, 130, 88, 10.1006/jsbi.2000.4221 · DOI · Paper page
- Chiti, 2006, Protein misfolding, functional amyloid, and human disease, Annu Rev Biochem, 75, 333, 10.1146/annurev.biochem.75.101304.123901 · DOI · Paper page
- Eisenberg, 2012, The amyloid state of proteins in human diseases, Cell, 148, 1188, 10.1016/j.cell.2012.02.022 · DOI · Paper page
- Knowles, 2010, Nanostructured films from hierarchical self-assembly of amyloidogenic proteins, Nat Nanotechnol, 5, 204, 10.1038/nnano.2010.26 · DOI · Paper page
- Watt, 2013, PMEL: a pigment cell-specific model for functional amyloid formation, Pigm Cell Melanoma R, 26, 300, 10.1111/pcmr.12067 · DOI
- 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
- 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
- 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
- Sagis, 2004, Mesoscopic properties of semiflexible amyloid fibrils, Langmuir, 20, 924, 10.1021/la035390s · DOI
- Akkermans, 2007, Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate, J Agric Food Chem, 55, 9877, 10.1021/jf0718897 · DOI
- 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
- Knowles, 2016, Amyloid fibrils as building blocks for natural and artificial functional materials, Adv Mater, 28, 6546, 10.1002/adma.201505961 · DOI · Paper page
- 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
- Bolisetty, 2016, Amyloid-carbon hybrid membranes for universal water purification, Nat Nanotechnol, 11, 365, 10.1038/nnano.2015.310 · DOI · Paper page
- Shen, 2017, Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron, Nat Nanotechnol, 12, 642, 10.1038/nnano.2017.58 · DOI · Paper page
- Bolisetty, 2019, Sustainable technologies for water purification from heavy metals: review and analysis, Chem Soc Rev, 48, 463, 10.1039/C8CS00493E · DOI · Paper page
- Veerman, 2003, A new multistep Ca2+-induced cold gelation process for beta-lactoglobulin, J Agric Food Chem, 51, 3880, 10.1021/jf0261396 · DOI
- 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
- 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
- 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
- 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
- Jimenez, 2002, The protofilament structure of insulin amyloid fibrils, Proc Natl Acad Sci USA, 99, 9196, 10.1073/pnas.142459399 · DOI · Paper page
- 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
- 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
- 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
- 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
- Sawaya, 2007, Atomic structures of amyloid cross-beta spines reveal varied steric zippers, Nature, 447, 453, 10.1038/nature05695 · DOI · Paper page
- Riek, 2016, The activities of amyloids from a structural perspective, Nature, 539, 227, 10.1038/nature20416 · DOI · Paper page
- 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
- 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
- Eisenberg, 2017, Structural studies of amyloid proteins at the molecular level, Annu Rev Biochem, 86, 69, 10.1146/annurev-biochem-061516-045104 · DOI
- 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
- Gremer, 2017, Fibril structure of amyloid-beta(1–42) by cryo-electron microscopy, Science, 358, 116, 10.1126/science.aao2825 · DOI · Paper page
- 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
- 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
- Lara, 2011, General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons, Biomacromolecules, 12, 1868, 10.1021/bm200216u · DOI
- 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
- Colvin, 2016, Atomic resolution structure of monomorphic Aβ(42) amyloid fibrils, J Am Chem Soc, 138, 9663, 10.1021/jacs.6b05129 · DOI · Paper page
- Wiltzius, 2009, Molecular mechanisms for protein-encoded inheritance, Nat Struct Mol Biol, 16, 973, 10.1038/nsmb.1643 · DOI · Paper page
- 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
- 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
- Hirota-Nakaoka, 2003, Dissolution of beta(2)-microglobulin amyloid fibrils by dimethylsulfoxide, J Biochem, 134, 159, 10.1093/jb/mvg124 · DOI
- Nelson, 2005, Structure of the cross-beta spine of amyloid-like fibrils, Nature, 435, 773, 10.1038/nature03680 · DOI · Paper page
- Tsemekhman, 2007, Cooperative hydrogen bonding in amyloid formation, Protein Sci, 16, 761, 10.1110/ps.062609607 · DOI
- 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
- 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
- Westermark, 1999, Staining methods for identification of amyloid in tissue, Methods Enzymol, 309, 3, 10.1016/S0076-6879(99)09003-5 · DOI · Paper page
- Stathopulos, 2004, Sonication of proteins causes formation of aggregates that resemble amyloid, Protein Sci, 13, 3017, 10.1110/ps.04831804 · DOI · Paper page
- Klunk, 1999, Quantifying amyloid by congo red spectral shift assay, Methods Enzymol, 309, 285, 10.1016/S0076-6879(99)09021-7 · DOI
- Bolognesi, 2010, Ans binding reveals common features of cytotoxic amyloid species, ACS Chem Biol, 5, 735, 10.1021/cb1001203 · DOI · Paper page
- 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
- 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
- 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
- Pinotsi, 2014, Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy, Nano Lett, 14, 339, 10.1021/nl4041093 · DOI
- 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
- 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
- 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
- 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
- Tycko, 2011, Solid-state NMR studies of amyloid fibril structure, Annu Rev Phys Chem, 62, 279, 10.1146/annurev-physchem-032210-103539 · DOI
- 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
- Lara, 2012, Self-assembly of ovalbumin into amyloid and non-amyloid fibrils, Biomacromolecules, 13, 4213, 10.1021/bm301481v · DOI
- 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
- 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
- Kavanagh, 2000, Heat-induced gelation of globular proteins: 4. Gelation kinetics of low ph beta-lactoglobulin gels, Langmuir, 16, 9584, 10.1021/la0004698 · DOI
- 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
- Gosal, 2002, Novel amyloid fibrillar networks derived from a globular protein: beta-lactoglobulin, Langmuir, 18, 7174, 10.1021/la025531a · DOI
- Arnaudov, 2003, Multiple steps during the formation of beta-lactoglobulin fibrils, Biomacromolecules, 4, 1614, 10.1021/bm034096b · DOI
- Bolisetty, 2011, Snapshots of fibrillation and aggregation kinetics in multistranded amyloid beta-lactoglobulin fibrils, Soft Matter, 7, 493, 10.1039/C0SM00502A · DOI
- 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
- 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
- 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
- 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
- Balchin, 2016, In vivo aspects of protein folding and quality control, Science, 353, aac4354, 10.1126/science.aac4354 · DOI · Paper page
- 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
- Fandrich, 2001, Amyloid fibrils from muscle myoglobin - even an ordinary globular protein can assume a rogue guise if conditions are right, Nature, 410, 165
- 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
- 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
- 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
- Gsponer, 2006, Theoretical approaches to protein aggregation, Protein Pept Lett, 13, 287, 10.2174/092986606775338407 · DOI
- Stefani, 2008, Protein folding and misfolding on surfaces, Int J Mol Sci, 9, 2515, 10.3390/ijms9122515 · DOI
- 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
- 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
- Uversky, 2008, Amyloidogenesis of natively unfolded proteins, Curr Alzheimer Res, 5, 260, 10.2174/156720508784533312 · DOI
- van der Linden, 2007, Self-assembly and aggregation of proteins, Curr Opin Colloid In, 12, 158, 10.1016/j.cocis.2007.07.010 · DOI
- 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
- 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
- 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
- Dobson, 1999, Protein misfolding, evolution and disease, Trends Biochem Sci, 24, 329, 10.1016/S0968-0004(99)01445-0 · DOI
- 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
- Gosal, 2004, Fibrillar beta-lactoglobulin gels: part 1. Fibril formation and structure, Biomacromolecules, 5, 2408, 10.1021/bm049659d · DOI
- 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
- 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
- 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
- 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
- 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
- Bolder, 2007, Effect of stirring and seeding on whey protein fibril formation, J Agric Food Chem, 55, 5661, 10.1021/jf063351r · DOI
- 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
- Akkermans, 2008, Enzyme-induced formation of beta-lactoglobulin fibrils by AspN endoproteinase, Food Biophys, 3, 390, 10.1007/s11483-008-9094-3 · DOI
- 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
- Hill, 2006, Shear flow induces amyloid fibril formation, Biomacromolecules, 7, 10, 10.1021/bm0505078 · DOI
- Dunstan, 2009, Shear-induced structure and mechanics of beta-lactoglobulin amyloid fibrils, Soft Matter, 5, 5020, 10.1039/b914089a · DOI
- 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
- 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
- Zappone, 2013, Catalytic activity of copper ions in the amyloid fibrillation of beta-lactoglobulin, Soft Matter, 9, 2412, 10.1039/c2sm27408f · DOI
- Guzzi, 2015, Ferric ions inhibit the amyloid fibrillation of beta-lactoglobulin at high temperature, Biomacromolecules, 16, 1794, 10.1021/acs.biomac.5b00371 · DOI
- Rasmussen, 2007, Formation of structured polymers upon controlled denaturation of beta-lactoglobulin with different chaotropes, Biopolymers, 86, 57, 10.1002/bip.20704 · DOI
- Goers, 2002, Conformational prerequisites for alpha-lactalbumin fibrillation, Biochemistry-Us, 41, 12546, 10.1021/bi0262698 · DOI
- Wang, 2011, Fibril formation of bovine alpha-lactalbumin is inhibited by glutathione, Food Biophys, 6, 138, 10.1007/s11483-010-9199-3 · DOI
- 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
- 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
- Graveland-Bikker, 2004, Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin, Langmuir, 20, 6841, 10.1021/la049579v · DOI
- 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
- 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
- Ipsen, 2007, Self-assembly of partially hydrolysed alpha-lactalbumin, Biotechnol Adv, 25, 602, 10.1016/j.biotechadv.2007.07.006 · DOI
- 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
- Knowles, 2007, Role of intermolecular forces in defining material properties of protein nanofibrils, Science, 318, 1900, 10.1126/science.1150057 · DOI · Paper page
- 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
- 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
- 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
- Koudelka, 2012, Methionine oxidation enhances kappa-casein amyloid fibril formation, J Agric Food Chem, 60, 4144, 10.1021/jf205168t · DOI
- 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
- 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
- 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
- Pan, 2015, Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties, Soft Matter, 11, 5898, 10.1039/C5SM01037C · DOI
- 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
- Koseki, 1989, Irreversible thermal denaturation and formation of linear aggregates of ovalbumin, Food Hydrocoll, 3, 123, 10.1016/S0268-005X(89)80022-0 · DOI
- 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
- 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
- Arnaudov, 2005, Thermally induced fibrillar aggregation of hen egg white lysozyme, Biophys J, 88, 515, 10.1529/biophysj.104.048819 · DOI · Paper page
- Lara, 2013, Towards lysozyme nanotube and 3D hybrid self-assembly, Nanoscale, 5, 7197, 10.1039/c3nr02194g · DOI
- 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
- Frare, 2004, A highly amyloidogenic region of hen lysozyme, J Mol Biol, 340, 1153, 10.1016/j.jmb.2004.05.056 · DOI · Paper page
- 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
- 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
- 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
- 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
- Vernaglia, 2004, Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme, Biomacromolecules, 5, 1362, 10.1021/bm0498979 · DOI
- Cao, 2004, Formation of amyloid fibrils from fully reduced hen egg white lysozyme, Protein Sci, 13, 319, 10.1110/ps.03183404 · DOI
- 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
- Wei, 2019, Assembly of iron-bound ovotransferrin amyloid fibrils, Food Hydrocoll, 89, 579, 10.1016/j.foodhyd.2018.11.028 · DOI
- Jurado, 2019, Apoferritin protein amyloid fibrils with tunable chirality and polymorphism, J Am Chem Soc, 141, 1606, 10.1021/jacs.8b11418 · DOI
- Usov, 2013, Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils, ACS Nano, 7, 10465, 10.1021/nn404886k · DOI
- Veerman, 2003, Mesostructure of fibrillar bovine serum albumin gels, Int J Biol Macromol, 31, 139, 10.1016/S0141-8130(02)00074-0 · DOI
- 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
- Holm, 2007, Aggregation and fibrillation of bovine serum albumin, Bba-Proteins Proteom, 1774, 1128, 10.1016/j.bbapap.2007.06.008 · DOI · Paper page
- 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
- Jayawardena, 2017, Amyloid fibrils from hemoglobin, Biomolecules, 7, 37, 10.3390/biom7020037 · DOI
- 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
- 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
- Huang, 2014, Self-assembly of rice bran globulin fibrils in electrostatic screening: nanostructure and gels, J Nanomater, 2014, 114, 10.1155/2014/951240 · DOI
- Ridgley, 2013, Evolution of the amyloid fiber over multiple length scales, ACS Nano, 7, 1006, 10.1021/nn303489a · DOI
- 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
- 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
- Ridgley, 2012, The effect of processing on large, self-assembled amyloid fibers, Soft Matter, 8, 10298, 10.1039/c2sm26496j · DOI
- Ridgley, 2014, The role of protein hydrophobicity in conformation change and self-assembly into large amyloid fibers, Biomacromolecules, 15, 1240, 10.1021/bm401815u · DOI
- 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
- 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
- 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
- Munialo, 2014, Fibril formation from pea protein and subsequent gel formation, J Agric Food Chem, 62, 2418, 10.1021/jf4055215 · DOI
- 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
- 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
- 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
- Kroes-Nijboer, 2011, Influence of protein hydrolysis on the growth kinetics of beta-lg fibrils, Langmuir, 27, 5753, 10.1021/la104797u · DOI
- Brown, 1992, Recent perspectives concerning the mechanism of H3O+-promoted and OH--promoted amide hydrolysis, Acc Chem Res, 25, 481, 10.1021/ar00023a001 · DOI
- Schultz, 1967, [28] cleavage at aspartic acid, vol. 11, 255, 10.1016/S0076-6879(67)11030-6 · DOI
- Adamcik, 2011, Adjustable twisting periodic pitch of amyloid fibrils, Soft Matter, 7, 5437, 10.1039/c1sm05382e · DOI
- 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
- Kroes-Nijboer, 2009, The critical aggregation concentration of beta-lactoglobulin-based fibril formation, Food Biophys, 4, 59, 10.1007/s11483-009-9101-3 · DOI
- Petkova, 2005, Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils, Science, 307, 262, 10.1126/science.1105850 · DOI · Paper page
- 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
- 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
- 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
- Vaneldik, 1989, Activation and reaction volumes in solution. 2, Chem Rev, 89, 549, 10.1021/cr00093a005 · DOI · Paper page
- 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
- Silva, 1993, Pressure stability of proteins, Annu Rev Phys Chem, 44, 89, 10.1146/annurev.pc.44.100193.000513 · DOI · Paper page
- Torrent, 2004, High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation, Biochemistry-Us, 43, 7162, 10.1021/bi049939d · DOI
- Jansen, 2004, High pressure promotes circularly shaped insulin amyloid, J Mol Biol, 338, 203, 10.1016/j.jmb.2004.02.056 · DOI
- 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
- Mishra, 2008, Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils, Angew Chem Int Ed, 47, 6518, 10.1002/anie.200802027 · DOI
- 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
- 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
- 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
- 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
- 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
- Jordens, 2011, Disassembly and reassembly of amyloid fibrils in water-ethanol mixtures, Biomacromolecules, 12, 187, 10.1021/bm101119t · DOI
- 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
- Veerman, 2002, Effect of electrostatic interactions on the percolation concentration of fibrillar beta-lactoglobulin gels, Biomacromolecules, 3, 869, 10.1021/bm025533+ · DOI
- 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
Tong, X., Cao, J., Tian, T., Lyu, B., Miao, L., Lian, Z., Cui, W., Liu, S., Wang, H., & Jiang, L. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107084 · Cited by 318
Impact of plasma reactive species on the structure and functionality of pea protein isolate
Bu, F., Nayak, G., Bruggeman, P., Annor, G., & Ismail, B. P. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2021.131135 · Cited by 105
Alrosan, M., Tan, T.-C., Easa, A. M., Gammoh, S., & Alu'datt, M. H. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1871589 · Cited by 104
Production and characterization of amaranth amyloid fibrils from food protein waste
Mykolenko, S., Soon, W. L., & Mezzenga, R. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109604 · Cited by 60
Self-citationWang, Z., Zeng, J., Deng, Y., Zhou, P., Li, P., Zhao, Z., Liu, G., & Zhang, M. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110621 · Cited by 38
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)
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications. https://app.cochat.ai/papers/10.1016/j.cis.2019.05.002
- The paper
- Cao, Y., & Mezzenga, R. (2019). Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications. Advances in Colloid and Interface Science. https://doi.org/10.1016/j.cis.2019.05.002
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.