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Volumn 16, Issue 1, 2013, Pages 29-39

Monitoring oligomer formation from self-aggregating amylin peptides using ESI-IMS-MS

Author keywords

Amyloid; Fibril; Ion mobility spectrometry mass spectrometry; Islet amyloid polypeptide; Molecular modelling

Indexed keywords

DIMERS; ELECTROSPRAY IONIZATION; GLYCOPROTEINS; ION MOBILITY SPECTROMETERS; MASS SPECTROMETRY; MOLECULAR MODELING;

EID: 84874522949     PISSN: 14356163     EISSN: 18654584     Source Type: Journal    
DOI: 10.1007/s12127-012-0115-z     Document Type: Article
Times cited : (15)

References (59)
  • 3
    • 70349730066 scopus 로고    scopus 로고
    • A new, higher resolution, ion mobility mass spectrometer
    • Kemper PR, Dupuis NF, Bowers MT (2009) A new, higher resolution, ion mobility mass spectrometer. Int J Mass Spectrom 287: 46-57.
    • (2009) Int J Mass Spectrom , vol.287 , pp. 46-57
    • Kemper, P.R.1    Dupuis, N.F.2    Bowers, M.T.3
  • 6
    • 23944446530 scopus 로고    scopus 로고
    • Recent developments in electrospray ionisation mass spectrometry: noncovalently bound protein complexes
    • Ashcroft AE (2005) Recent developments in electrospray ionisation mass spectrometry: noncovalently bound protein complexes. Nat Prod Rep 22: 452-464.
    • (2005) Nat Prod Rep , vol.22 , pp. 452-464
    • Ashcroft, A.E.1
  • 8
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: technology for structural genomics and proteomics
    • Benesch JL, Ruotolo BT, Simmons DA, Robinson CV (2007) Protein complexes in the gas phase: technology for structural genomics and proteomics. Chem Rev 107: 3544-3567.
    • (2007) Chem Rev , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 9
    • 70349876855 scopus 로고    scopus 로고
    • Mass spectrometry of large complexes
    • Bich C, Zenobi R (2009) Mass spectrometry of large complexes. Curr Opin Chem Biol 19: 632-639.
    • (2009) Curr Opin Chem Biol , vol.19 , pp. 632-639
    • Bich, C.1    Zenobi, R.2
  • 10
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: a bridge between interactomics and structural biology
    • Heck AJ (2008) Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 11: 927-933.
    • (2008) Nat Methods , vol.11 , pp. 927-933
    • Heck, A.J.1
  • 11
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo JA (1997) Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom Rev 16: 1-23.
    • (1997) Mass Spectrom Rev , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 12
    • 77951081386 scopus 로고    scopus 로고
    • Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • Smith DP, Radford SE, Ashcroft AE (2010) Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc Natl Acad Sci USA 107: 6794-6798.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 15
    • 77953912267 scopus 로고    scopus 로고
    • Mass spectrometry and the amyloid problem-how far can we go in the gas phase?
    • Ashcroft AE (2010) Mass spectrometry and the amyloid problem-how far can we go in the gas phase? J Am Soc Mass Spectrom 21: 1087-1096.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1087-1096
    • Ashcroft, A.E.1
  • 16
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the international society of amyloidosis
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P (2010) Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the international society of amyloidosis. Amyloid 17: 101-104.
    • (2010) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 17
    • 79955761085 scopus 로고    scopus 로고
    • Structural insights into functional and pathological amyloid
    • Shewmaker F, McGlinchey RP, Wickner RB (2011) Structural insights into functional and pathological amyloid. J Biol Chem 286: 16533-16540.
    • (2011) J Biol Chem , vol.286 , pp. 16533-16540
    • Shewmaker, F.1    McGlinchey, R.P.2    Wickner, R.B.3
  • 18
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA (2004) Protein aggregation and neurodegenerative disease. Nat Methods 10: 10-17.
    • (2004) Nat Methods , vol.10 , pp. 10-17
    • Ross, C.A.1    Poirier, M.A.2
  • 19
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Ann Rev Biochem 75: 333-366.
    • (2006) Ann Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 20
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Ann Rev Neurosci 26: 267-298.
    • (2003) Ann Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 21
    • 79959342196 scopus 로고    scopus 로고
    • Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity
    • Last NB, Rhoades E, Miranker AD (2011) Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity. Proc Natl Acad Sci USA 108: 9460-9465.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9460-9465
    • Last, N.B.1    Rhoades, E.2    Miranker, A.D.3
  • 22
    • 80052508937 scopus 로고    scopus 로고
    • Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly
    • Smith DP, Woods LA, Radford SE, Ashcroft AE (2011) Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly. Biophys J 101: 1238-1247.
    • (2011) Biophys J , vol.101 , pp. 1238-1247
    • Smith, D.P.1    Woods, L.A.2    Radford, S.E.3    Ashcroft, A.E.4
  • 24
    • 73249115986 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor
    • Dupuis NF, Wu C, Shea J-E, Bowers MT (2009) Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor. J Am Chem Soc 131: 18283-18292.
    • (2009) J Am Chem Soc , vol.131 , pp. 18283-18292
    • Dupuis, N.F.1    Wu, C.2    Shea, J.-E.3    Bowers, M.T.4
  • 25
    • 79955896407 scopus 로고    scopus 로고
    • The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces
    • Dupuis NF, Wu C, Shea JE, Bowers MT (2011) The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces. J Am Chem Soc 133: 7240-7243.
    • (2011) J Am Chem Soc , vol.133 , pp. 7240-7243
    • Dupuis, N.F.1    Wu, C.2    Shea, J.E.3    Bowers, M.T.4
  • 26
    • 74949142621 scopus 로고    scopus 로고
    • Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation
    • Grabenauer M, Wu C, Soto P, Shea JE, Bowers MT (2009) Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation. J Am Chem Soc 132: 532-539.
    • (2009) J Am Chem Soc , vol.132 , pp. 532-539
    • Grabenauer, M.1    Wu, C.2    Soto, P.3    Shea, J.E.4    Bowers, M.T.5
  • 27
    • 0025858451 scopus 로고
    • Islet amyloid polypeptide (IAPP). A short review
    • Stridsberg M, Wilander E (1991) Islet amyloid polypeptide (IAPP). A short review. Acta Oncol 30: 451-456.
    • (1991) Acta Oncol , vol.30 , pp. 451-456
    • Stridsberg, M.1    Wilander, E.2
  • 28
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • Westermark P, Andersson A, Westermark GT (2011) Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiol Rev 91: 795-826.
    • (2011) Physiol Rev , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 30
    • 0034001363 scopus 로고    scopus 로고
    • Direct measurement of islet amyloid polypeptide fibrillogenesis by mass spectrometry
    • Larson JL, Ko E, Miranker AD (2000) Direct measurement of islet amyloid polypeptide fibrillogenesis by mass spectrometry. Prot Sci 9: 427-431.
    • (2000) Prot Sci , vol.9 , pp. 427-431
    • Larson, J.L.1    Ko, E.2    Miranker, A.D.3
  • 31
    • 79955852760 scopus 로고    scopus 로고
    • Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils
    • Zhao J, Yu X, Liang G, Zheng J (2011) Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils. Biomacromolecules 12: 1781-1784.
    • (2011) Biomacromolecules , vol.12 , pp. 1781-1784
    • Zhao, J.1    Yu, X.2    Liang, G.3    Zheng, J.4
  • 33
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin 20-29
    • Moriarty DF, Raleigh DP (1999) Effects of sequential proline substitutions on amyloid formation by human amylin 20-29. Biochemistry 38: 1811-1818.
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 34
    • 0023787576 scopus 로고
    • Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein
    • Glenner GG, Eanes D, Wiley C (1988) Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein. Biochem Biophys Res Commun 155: 608-614.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 608-614
    • Glenner, G.G.1    Eanes, D.2    Wiley, C.3
  • 37
    • 0033473749 scopus 로고    scopus 로고
    • A database of 660 peptide ion cross sections: use of intrinsic size parameters for bona fide predictions of cross sections
    • Valentine SJ, Counterman AE, Clemmer DE (1999) A database of 660 peptide ion cross sections: use of intrinsic size parameters for bona fide predictions of cross sections. J Am Soc Mass Spectrom 10: 1188-1211.
    • (1999) J Am Soc Mass Spectrom , vol.10 , pp. 1188-1211
    • Valentine, S.J.1    Counterman, A.E.2    Clemmer, D.E.3
  • 38
    • 41149162020 scopus 로고    scopus 로고
    • Fibril growth kinetics reveal a region of beta 2-microglobulin important for nucleation and elongation of aggregation
    • Platt GW, Routledge KE, Homans SW, Radford SE (2008) Fibril growth kinetics reveal a region of beta 2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol 378: 251-263.
    • (2008) J Mol Biol , vol.378 , pp. 251-263
    • Platt, G.W.1    Routledge, K.E.2    Homans, S.W.3    Radford, S.E.4
  • 39
    • 57349120654 scopus 로고    scopus 로고
    • Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction
    • Madine J, Jack E, Stockley PG, Radford SE, Serpell LC, Middleton DA (2008) Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction. J Am Chem Soc 130: 14990-15001.
    • (2008) J Am Chem Soc , vol.130 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Stockley, P.G.3    Radford, S.E.4    Serpell, L.C.5    Middleton, D.A.6
  • 40
    • 79251507307 scopus 로고    scopus 로고
    • Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture
    • Middleton DA (2011) Solid-state NMR detection of 14N-13C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture. Magn Reson Chem 49: 65-69.
    • (2011) Magn Reson Chem , vol.49 , pp. 65-69
    • Middleton, D.A.1
  • 41
    • 0345983583 scopus 로고    scopus 로고
    • Modelling unusual nucleic acid structures
    • N. B. Leontes and J. SantaLuciaJr (Eds.), Washington, DC: American Chemical Society
    • Macke T, Case DA (1998) Modelling unusual nucleic acid structures. In: Leontes NB, SantaLucia J Jr (eds) Molecular modelling of nucleic acids. American Chemical Society, Washington, DC, pp 379-393.
    • (1998) Molecular Modelling of Nucleic Acids , pp. 379-393
    • Macke, T.1    Case, D.A.2
  • 44
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple amber force fields and development of improved backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C (2006) Comparison of multiple amber force fields and development of improved backbone parameters. Proteins 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 45
    • 33748887803 scopus 로고    scopus 로고
    • Structural information from ion mobility measurements: effects of the long-range potential
    • Mesleh MF, Hunter JM, Shvartsburg AA, Schatz GC, Jarrold MF (1996) Structural information from ion mobility measurements: effects of the long-range potential. J Phys Chem 100: 16082-16086.
    • (1996) J Phys Chem , vol.100 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 46
    • 0001373159 scopus 로고
    • Interspecies variations affect the kinetics and thermodynamics of amyloid plaque formation; peptide models of pancreatic amyloid
    • Ashburn TT, Lansbury PT (1993) Interspecies variations affect the kinetics and thermodynamics of amyloid plaque formation; peptide models of pancreatic amyloid. J Am Chem Soc 115: 11012-11013.
    • (1993) J Am Chem Soc , vol.115 , pp. 11012-11013
    • Ashburn, T.T.1    Lansbury, P.T.2
  • 49
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
    • Bleiholder C, Dupuis NF, Wyttenback T, Bowers MT (2011) Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation. Nat Chem 3: 172-177.
    • (2011) Nat Chem , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenback, T.3    Bowers, M.T.4
  • 51
    • 77955755403 scopus 로고    scopus 로고
    • Recoupling of native homonuclear dipolar couplings in magic-angle-spinning solid-state NMR by the double-oscillating field technique
    • Straaso LA, Nielsen NC (2010) Recoupling of native homonuclear dipolar couplings in magic-angle-spinning solid-state NMR by the double-oscillating field technique. J Chem Phys 133: 064501.
    • (2010) J Chem Phys , vol.133 , pp. 064501
    • Straaso, L.A.1    Nielsen, N.C.2
  • 52
    • 33750294048 scopus 로고    scopus 로고
    • Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry
    • Smith AM, Jahn TR, Ashcroft AE, Radford SE (2006) Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol 364: 9-19.
    • (2006) J Mol Biol , vol.364 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 53
    • 84874535179 scopus 로고    scopus 로고
    • World Health Organisation,Accessed 6 Nov 2012
    • World Health Organisation (2012) http://www. who. int/features/factfiles/diabetes. Accessed 6 Nov 2012.
    • (2012)
  • 55
    • 84859379008 scopus 로고    scopus 로고
    • Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols
    • Cao P, Raleigh DP (2012) Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry 51: 2670-2683.
    • (2012) Biochemistry , vol.51 , pp. 2670-2683
    • Cao, P.1    Raleigh, D.P.2
  • 57
    • 84255160885 scopus 로고    scopus 로고
    • Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: possible link between coffee consumption and diabetes mellitus
    • Cheng B, Liu X, Gong H, Huang L, Chen H, Zhang X, Li C, Yang M, Ma B, Jiao L, Zheng L, Huang K (2011) Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: possible link between coffee consumption and diabetes mellitus. J Agric Food Chem 59: 13147-13155.
    • (2011) J Agric Food Chem , vol.59 , pp. 13147-13155
    • Cheng, B.1    Liu, X.2    Gong, H.3    Huang, L.4    Chen, H.5    Zhang, X.6    Li, C.7    Yang, M.8    Ma, B.9    Jiao, L.10    Zheng, L.11    Huang, K.12


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