메뉴 건너뛰기




Volumn 102, Issue 5, 2012, Pages 1154-1162

Enrichment of amyloidogenesis at an air-water interface

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; PEPTIDE FRAGMENT; WATER;

EID: 84863240972     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.01.041     Document Type: Article
Times cited : (57)

References (33)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • DOI 10.1146/annurev.biochem.66.1.385
    • J.D. Harper, and P.T. Lansbury Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407 (Pubitemid 27274662)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 3
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation
    • B. Soreghan, J. Kosmoski, and C. Glabe Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation J. Biol. Chem. 269 1994 28551 28554 (Pubitemid 24366683)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.46 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 4
    • 2342641617 scopus 로고    scopus 로고
    • Rapid method for measurement of surface tension in multiwell plates
    • DOI 10.1038/labinvest.3700054
    • M.G. Cottingham, C.D. Bain, and D.J. Vaux Rapid method for measurement of surface tension in multiwell plates Lab. Invest. 84 2004 523 529 (Pubitemid 41656480)
    • (2004) Laboratory Investigation , vol.84 , Issue.4 , pp. 523-529
    • Cottingham, M.G.1    Bain, C.D.2    Vaux, D.J.T.3
  • 5
    • 36049013172 scopus 로고    scopus 로고
    • Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy
    • DOI 10.1529/biophysj.107.110635
    • D.H. Lopes, and A. Meister R. Winter Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy Biophys. J. 93 2007 3132 3141 (Pubitemid 350097104)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3132-3141
    • Lopes, D.H.J.1    Meister, A.2    Gohlke, A.3    Hauser, A.4    Blume, A.5    Winter, R.6
  • 6
    • 70350183804 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: Capacity scaling with adsorbate molecular weight and adsorbent surface energy
    • P. Parhi, and A. Golas E.A. Vogler Volumetric interpretation of protein adsorption: capacity scaling with adsorbate molecular weight and adsorbent surface energy Biomaterials 30 2009 6814 6824
    • (2009) Biomaterials , vol.30 , pp. 6814-6824
    • Parhi, P.1    Golas, A.2    Vogler, E.A.3
  • 7
    • 0027228051 scopus 로고
    • Induction of changes in the secondary structure of globular proteins by a hydrophobic surface
    • H. Wu, and Y. Fan S.F. Sui Induction of changes in the secondary structure of globular proteins by a hydrophobic surface Eur. Biophys. J. 22 1993 201 205 (Pubitemid 23279499)
    • (1993) European Biophysics Journal , vol.22 , Issue.3 , pp. 201-205
    • Wu, H.1    Fan, Y.2    Sheng, J.3    Sui, S.-F.4
  • 8
    • 0344082808 scopus 로고    scopus 로고
    • Traube-rule interpretation of protein adsorption at the liquid-vapor interface
    • A. Krishnan, C.A. Siedlecki, and E.A. Vogler Traube-rule interpretation of protein adsorption at the liquid-vapor interface Langmuir 19 2003 10342 10352
    • (2003) Langmuir , vol.19 , pp. 10342-10352
    • Krishnan, A.1    Siedlecki, C.A.2    Vogler, E.A.3
  • 9
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 10
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.02.021, PII S0005273606000733
    • H. Sato, and J.B. Feix Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1245 1256 (Pubitemid 44444829)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 11
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes
    • DOI 10.1021/bi971843e
    • E. Terzi, G. Hölzemann, and J. Seelig Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes Biochemistry 36 1997 14845 14852 (Pubitemid 27524407)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14845-14852
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 12
    • 75149180052 scopus 로고    scopus 로고
    • Competing discrete interfacial effects are critical for amyloidogenesis
    • L. Jean, and C.F. Lee D.J. Vaux Competing discrete interfacial effects are critical for amyloidogenesis FASEB J. 24 2010 309 317
    • (2010) FASEB J. , vol.24 , pp. 309-317
    • Jean, L.1    Lee, C.F.2    Vaux, D.J.3
  • 13
    • 77952775252 scopus 로고    scopus 로고
    • Amyloid-β fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly
    • E.Y. Chi, and S.L. Frey K.Y. Lee Amyloid-β fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly Biophys. J. 98 2010 2299 2308
    • (2010) Biophys. J. , vol.98 , pp. 2299-2308
    • Chi, E.Y.1    Frey, S.L.2    Lee, K.Y.3
  • 14
    • 65249097290 scopus 로고    scopus 로고
    • A kinetic model for β-amyloid adsorption at the air/solution interface and its implication to the β-amyloid aggregation process
    • D. Jiang, and K.L. Dinh F. Zhou A kinetic model for β-amyloid adsorption at the air/solution interface and its implication to the β-amyloid aggregation process J. Phys. Chem. B 113 2009 3160 3168
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3160-3168
    • Jiang, D.1    Dinh, K.L.2    Zhou, F.3
  • 15
    • 76849106756 scopus 로고    scopus 로고
    • Critical role of interfaces and agitation on the nucleation of Aβ amyloid fibrils at low concentrations of Aβ monomers
    • A. Morinaga, and K. Hasegawa H. Naiki Critical role of interfaces and agitation on the nucleation of Aβ amyloid fibrils at low concentrations of Aβ monomers Biochim. Biophys. Acta 1804 2010 986 995
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 986-995
    • Morinaga, A.1    Hasegawa, K.2    Naiki, H.3
  • 16
    • 79955549335 scopus 로고    scopus 로고
    • Recruitment of class i hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation
    • V.K. Morris, and Q. Ren M. Sunde Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation J. Biol. Chem. 286 2011 15955 15963
    • (2011) J. Biol. Chem. , vol.286 , pp. 15955-15963
    • Morris, V.K.1    Ren, Q.2    Sunde, M.3
  • 17
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of β-amyloid peptide
    • C.L. Shen, and R.M. Murphy Solvent effects on self-assembly of β-amyloid peptide Biophys. J. 69 1995 640 651
    • (1995) Biophys. J. , vol.69 , pp. 640-651
    • Shen, C.L.1    Murphy, R.M.2
  • 18
    • 0028168336 scopus 로고
    • Amyloid-β aggregation: Selective inhibition of aggregation in mixtures of amyloid with different chain lengths
    • S.W. Snyder, and U.S. Ladror T.F. Holzman Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths Biophys. J. 67 1994 1216 1228
    • (1994) Biophys. J. , vol.67 , pp. 1216-1228
    • Snyder, S.W.1    Ladror, U.S.2    Holzman, T.F.3
  • 20
    • 33947369859 scopus 로고    scopus 로고
    • Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology
    • DOI 10.1021/bi0621967
    • P. Marek, and A. Abedini D.P. Raleigh Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology Biochemistry 46 2007 3255 3261 (Pubitemid 46449146)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3255-3261
    • Marek, P.1    Abedini, A.2    Song, B.3    Kanungo, M.4    Johnson, M.E.5    Gupta, R.6    Zaman, W.7    Wong, S.S.8    Raleigh, D.P.9
  • 21
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • DOI 10.1016/j.jmb.2004.06.086, PII S0022283604007983
    • J.D. Knight, and A.D. Miranker Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol. 341 2004 1175 1187 (Pubitemid 39099208)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 22
    • 43049164334 scopus 로고    scopus 로고
    • Secondary nucleation and accessible surface in insulin amyloid fibril formation
    • V. Foderà, and F. Librizzi M. Leone Secondary nucleation and accessible surface in insulin amyloid fibril formation J. Phys. Chem. B 112 2008 3853 3858
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3853-3858
    • Foderà, V.1    Librizzi, F.2    Leone, M.3
  • 23
    • 70349503652 scopus 로고    scopus 로고
    • Isotropic-nematic phase transition in amyloid fibrillization
    • C.F. Lee Isotropic-nematic phase transition in amyloid fibrillization Phys. Rev. E. 80 2009 031902
    • (2009) Phys. Rev. E. , vol.80 , pp. 031902
    • Lee, C.F.1
  • 24
    • 25444522601 scopus 로고    scopus 로고
    • Thermodynamics of Aβ(1-40) amyloid fibril elongation
    • DOI 10.1021/bi050927h
    • B. O'Nuallain, and S. Shivaprasad R. Wetzel Thermodynamics of A β(1-40) amyloid fibril elongation Biochemistry 44 2005 12709 12718 (Pubitemid 41377310)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12709-12718
    • O'Nuallain, B.1    Shivaprasad, S.2    Kheterpal, I.3    Wetzel, R.4
  • 25
    • 27744511311 scopus 로고    scopus 로고
    • The wettability of polytetrafluoroethylene and polymethyl methacrylate by aqueous solution of two cationic surfactants mixture
    • DOI 10.1016/j.jcis.2005.06.038, PII S0021979705006983
    • K. Szymczyk, and A. Zdziennicka W. Wójcik The wettability of polytetrafluoroethylene and polymethyl methacrylate by aqueous solution of two cationic surfactants mixture J. Colloid Interface Sci. 293 2006 172 180 (Pubitemid 41635348)
    • (2006) Journal of Colloid and Interface Science , vol.293 , Issue.1 , pp. 172-180
    • Szymczyk, K.1    Zdziennicka, A.2    Janczuk, B.3    Wojcik, W.4
  • 28
    • 70349976982 scopus 로고    scopus 로고
    • Self-assembly of protein amyloids: A competition between amorphous and ordered aggregation
    • C.F. Lee Self-assembly of protein amyloids: a competition between amorphous and ordered aggregation Phys. Rev. E. 80 2009 031922
    • (2009) Phys. Rev. E. , vol.80 , pp. 031922
    • Lee, C.F.1
  • 30
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • H. LeVine 3rd Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution Protein Sci. 2 1993 404 410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine III, H.1
  • 31
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • T.P. Knowles, and A.W. Fitzpatrick M.E. Welland Role of intermolecular forces in defining material properties of protein nanofibrils Science 318 2007 1900 1903
    • (2007) Science , vol.318 , pp. 1900-1903
    • Knowles, T.P.1    Fitzpatrick, A.W.2    Welland, M.E.3
  • 32
    • 0344687319 scopus 로고    scopus 로고
    • The mechanism of insulin action on islet amyloid polypeptide fiber formation
    • DOI 10.1016/j.jmb.2003.10.045
    • J.L. Larson, and A.D. Miranker The mechanism of insulin action on islet amyloid polypeptide fiber formation J. Mol. Biol. 335 2004 221 231 (Pubitemid 37494974)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.1 , pp. 221-231
    • Larson, J.L.1    Miranker, A.D.2
  • 33
    • 43049173602 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase
    • N. Barnthip, and H. Noh E.A. Vogler Volumetric interpretation of protein adsorption: kinetic consequences of a slowly-concentrating interphase Biomaterials 29 2008 3062 3074
    • (2008) Biomaterials , vol.29 , pp. 3062-3074
    • Barnthip, N.1    Noh, H.2    Vogler, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.