메뉴 건너뛰기




Volumn 20, Issue 9, 2010, Pages 571-579

Tuning the properties of β-lactoglobulin nanofibrils with pH, NaCl and CaCl2

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIL FORMATION; FIBRIL MORPHOLOGY; GROWTH PHASE; LACTOGLOBULIN; LAG PHASE; NANO-FIBRILS; PERSISTENCE LENGTH; SALT CONCENTRATION;

EID: 77954819394     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2010.02.014     Document Type: Article
Times cited : (119)

References (40)
  • 2
    • 44449138916 scopus 로고    scopus 로고
    • Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2
    • Akkermans C., Venema P., van der Goot A.J., Gruppen H., Bakx E.J., Boom R.M., et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules 2008, 9:1474-1479.
    • (2008) Biomacromolecules , vol.9 , pp. 1474-1479
    • Akkermans, C.1    Venema, P.2    van der Goot, A.J.3    Gruppen, H.4    Bakx, E.J.5    Boom, R.M.6
  • 3
    • 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. Biophysical Journal 2005, 88:515-526.
    • (2005) Biophysical Journal , vol.88 , pp. 515-526
    • Arnaudov, L.N.1    de Vries, R.2
  • 4
    • 33846274983 scopus 로고    scopus 로고
    • Strong impact of ionic strength on the kinetics of fibrillar aggregation of bovine β-lactoglobulin
    • Arnaudov L.N., de Vries R. Strong impact of ionic strength on the kinetics of fibrillar aggregation of bovine β-lactoglobulin. Biomacromolecules 2006, 7:3490-3498.
    • (2006) Biomacromolecules , vol.7 , pp. 3490-3498
    • Arnaudov, L.N.1    de Vries, R.2
  • 5
    • 34247257911 scopus 로고    scopus 로고
    • Theoretical modeling of the kinetics of fibrillar aggregation of bovine β-lactoglobulin at pH 2
    • Arnaudov L.N., de Vries R. Theoretical modeling of the kinetics of fibrillar aggregation of bovine β-lactoglobulin at pH 2. Journal of Chemistry and Physics 2007, 126.
    • (2007) Journal of Chemistry and Physics , vol.126
    • Arnaudov, L.N.1    de Vries, R.2
  • 6
    • 0001417865 scopus 로고    scopus 로고
    • Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2
    • Aymard P., Nicolai T., Durand D., Clark A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 1999, 32:2542-2552.
    • (1999) Macromolecules , vol.32 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3    Clark, A.4
  • 7
    • 0034623193 scopus 로고    scopus 로고
    • Electrostatic potential profiles may guide cation-pi interaction in antimalarials chloroquine and mefloquine: an ab initio quantum chemical study
    • Bhattacharjee A.K. Electrostatic potential profiles may guide cation-pi interaction in antimalarials chloroquine and mefloquine: an ab initio quantum chemical study. Journal of Molecular Structure: THEOCHEM 2000, 529:193-201.
    • (2000) Journal of Molecular Structure: THEOCHEM , vol.529 , pp. 193-201
    • Bhattacharjee, A.K.1
  • 9
    • 33947694371 scopus 로고    scopus 로고
    • Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation
    • Bolder S.G., Vasbinder A.J., Sagis L.M.C., van der Linden E. Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. International Dairy Journal 2007, 17:846-853.
    • (2007) International Dairy Journal , vol.17 , pp. 846-853
    • Bolder, S.G.1    Vasbinder, A.J.2    Sagis, L.M.C.3    van der Linden, E.4
  • 10
  • 11
    • 3343005633 scopus 로고    scopus 로고
    • Differences and limits in estimates of persistence length for semi-flexible macromolecules
    • Cifra P. Differences and limits in estimates of persistence length for semi-flexible macromolecules. Polymer 2004, 45:5995-6002.
    • (2004) Polymer , vol.45 , pp. 5995-6002
    • Cifra, P.1
  • 12
    • 0030033588 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of Benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-pi interactions in chemistry and biology: a new view of Benzene, Phe, Tyr, and Trp. Science 1996, 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 14
    • 34047132881 scopus 로고    scopus 로고
    • Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study
    • Euston S.R., Ur-Rehman S., Costello G. Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study. Food Hydrocolloids 2007, 21:1081-1091.
    • (2007) Food Hydrocolloids , vol.21 , pp. 1081-1091
    • Euston, S.R.1    Ur-Rehman, S.2    Costello, G.3
  • 15
    • 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. Cellular and Molecular Life Sciences 2007, 64:2066-2078.
    • (2007) Cellular and Molecular Life Sciences , vol.64 , pp. 2066-2078
    • Fändrich, M.1
  • 16
    • 9744228666 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure
    • Gosal W.S., Clark A.H., Ross-Murphy S.B. Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure. Biomacromolecules 2004, 5:2408-2419.
    • (2004) Biomacromolecules , vol.5 , pp. 2408-2419
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 17
    • 4043078473 scopus 로고    scopus 로고
    • Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin
    • Graveland-Bikker J.F., Ipsen R., Otte J., de Kruif C.G. Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin. Langmuir 2004, 20:6841-6846.
    • (2004) Langmuir , vol.20 , pp. 6841-6846
    • Graveland-Bikker, J.F.1    Ipsen, R.2    Otte, J.3    de Kruif, C.G.4
  • 20
    • 73649116661 scopus 로고    scopus 로고
    • Liquid crystalline phase behavior of protein fibers in water: experiments versus theory
    • Jung J.M., Mezzenga R. Liquid crystalline phase behavior of protein fibers in water: experiments versus theory. Langmuir 2010, 26:504-514.
    • (2010) Langmuir , vol.26 , pp. 504-514
    • Jung, J.M.1    Mezzenga, R.2
  • 23
    • 0034318911 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels
    • Kavanagh G.M., Clark A.H., Ross-Murphy S.B. Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels. Langmuir 2000, 16:9584-9594.
    • (2000) Langmuir , vol.16 , pp. 9584-9594
    • Kavanagh, G.M.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 25
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH
    • Langton M., Hermansson A.M. Fine-stranded and particulate gels of β-lactoglobulin and whey-protein at varying pH. Food Hydrocolloids 1992, 5:523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.M.2
  • 27
    • 0031823022 scopus 로고    scopus 로고
    • Theoretical models of viscoelasticity of actin solutions and the actin cortex
    • Mackintosh F.C. Theoretical models of viscoelasticity of actin solutions and the actin cortex. Biological Bulletin 1998, 194:351-353.
    • (1998) Biological Bulletin , vol.194 , pp. 351-353
    • Mackintosh, F.C.1
  • 28
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
    • Mishra R., Sörgjerd K., Nyström S., Nordigården A., Yu Y.-C., Hammarström P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. Journal of Molecular Biology 2007, 366:1029-1044.
    • (2007) Journal of Molecular Biology , vol.366 , pp. 1029-1044
    • Mishra, R.1    Sörgjerd, K.2    Nyström, S.3    Nordigården, A.4    Yu, Y.-C.5    Hammarström, P.6
  • 29
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, Minimal/" Ockham's Razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • Morris A.M., Watzky M.A., Agar J.N., Finke R.G. Fitting neurological protein aggregation kinetic data via a 2-step, Minimal/" Ockham's Razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth. Biochemistry 2008, 47:2413-2427.
    • (2008) Biochemistry , vol.47 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 30
    • 67349276424 scopus 로고    scopus 로고
    • Cold-set thickening mechanism of β-lactoglobulin at low pH: concentration effects
    • Mudgal P., Daubert C.R., Foegeding E.A. Cold-set thickening mechanism of β-lactoglobulin at low pH: concentration effects. Food Hydrocolloids 2009, 23:1762-1770.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1762-1770
    • Mudgal, P.1    Daubert, C.R.2    Foegeding, E.A.3
  • 31
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H., Nakakuki K. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Laboratory Investigation 1996, 74:374-383.
    • (1996) Laboratory Investigation , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 32
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
    • Nielsen L., Frokjaer S., Carpenter J.F., Brange J. Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy. Journal of Pharmaceutical Sciences 2001, 90:29-37.
    • (2001) Journal of Pharmaceutical Sciences , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 33
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001, 40:6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6
  • 34
    • 19544375553 scopus 로고    scopus 로고
    • Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations
    • de la Paz M.L., de Mori G.M.S., Serrano L., Colombo G. Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations. Journal of Molecular Biology 2005, 349:583-596.
    • (2005) Journal of Molecular Biology , vol.349 , pp. 583-596
    • de la Paz, M.L.1    de Mori, G.M.S.2    Serrano, L.3    Colombo, G.4
  • 35
    • 8644266740 scopus 로고    scopus 로고
    • X-ray and light scattering study of the structure of large protein aggregates at neutral pH
    • Pouzot M., Nicolai T., Visschers R.W., Weijers M. X-ray and light scattering study of the structure of large protein aggregates at neutral pH. Food Hydrocolloids 2005, 19:231-238.
    • (2005) Food Hydrocolloids , vol.19 , pp. 231-238
    • Pouzot, M.1    Nicolai, T.2    Visschers, R.W.3    Weijers, M.4
  • 36
    • 26844482366 scopus 로고    scopus 로고
    • +] interactions with the aromatic
    • +] interactions with the aromatic motifs of naturally occurring amino acids: a theoretical study. Journal of Physical Chemistry 2005, 109:8893-8903.
    • (2005) Journal of Physical Chemistry , vol.109 , pp. 8893-8903
    • Reddy, A.S.1    Sastry, G.N.2
  • 38
    • 1242310516 scopus 로고    scopus 로고
    • Mesoscopic properties of semiflexible amyloid fibrils
    • Sagis L.M.C., Veerman C., van der Linden E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 2004, 20:924-927.
    • (2004) Langmuir , vol.20 , pp. 924-927
    • Sagis, L.M.C.1    Veerman, C.2    van der Linden, E.3
  • 39
    • 0033846408 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration
    • Schokker E.P., Singh H., Pinder D.N., Creamer L.K. Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. International Dairy Journal 2000, 10:233-240.
    • (2000) International Dairy Journal , vol.10 , pp. 233-240
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Creamer, L.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.