메뉴 건너뛰기




Volumn 4, Issue 4, 1997, Pages 240-252

Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid β-peptide

Author keywords

Amyloidosis; Nuclear magnetic resonance; Trifluoroacetic acid; peptide

Indexed keywords


EID: 0001146033     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506129709003835     Document Type: Article
Times cited : (112)

References (64)
  • 1
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • Selkoe DJ (1994). Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17, 489-517
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 4
    • 0029670381 scopus 로고    scopus 로고
    • The βA4 amyloid precursor protein gene and Alzheimer's Disease
    • Hendriks L and Van Broeckhoven C (1996). The βA4 amyloid precursor protein gene and Alzheimer's Disease. Eur. J. Biochem. 237, 6-15
    • (1996) Eur. J. Biochem. , vol.237 , pp. 6-15
    • Hendriks, L.1    Van Broeckhoven, C.2
  • 5
    • 0029833865 scopus 로고    scopus 로고
    • β-amyloid precursor protein
    • Tischer E and Cordell B (1996). β-amyloid precursor protein. J. Biol. Chem. 271, 21914-21919
    • (1996) J. Biol. Chem. , vol.271 , pp. 21914-21919
    • Tischer, E.1    Cordell, B.2
  • 6
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of β-amyloid in Alzheimer's diseased tissue by synchroton fourier transform infrared microspectroscopy
    • Choo L-Pi, Wetzel DL, Halliday WC, Jackson M, LeVine SM and Mantsch HH (1996). In situ characterization of β-amyloid in Alzheimer's diseased tissue by synchroton fourier transform infrared microspectroscopy. Biophys. J. 71, 1672-1679
    • (1996) Biophys. J. , vol.71 , pp. 1672-1679
    • Choo, L.-Pi.1    Wetzel, D.L.2    Halliday, W.C.3    Jackson, M.4    LeVine, S.M.5    Mantsch, H.H.6
  • 7
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's Disease
    • Halverson K, Fraser PE, Kirschner DA and Lansbury PT (1990). Molecular determinants of amyloid deposition in Alzheimer's Disease. Biochemistry 29, 2639-2644
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury, P.T.4
  • 8
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow CJ and Zagorski MG (1991). Solution structures of β peptide and its constituent fragments: relation to amyloid deposition. Science 253, 179-182
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 9
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's Disease
    • Hilbich C, Kisters-Woide B, Reed J, Masters CL and Beyreuther K (1991). Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's Disease. J. Mol. Biol. 218, 149-163
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woide, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 10
    • 0027989805 scopus 로고
    • Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide
    • Shen C-L, Fitzgerald MC and Murphy RM (1994). Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide. Biophys. J. 67, 1238-1246
    • (1994) Biophys. J. , vol.67 , pp. 1238-1246
    • Shen, C.-L.1    Fitzgerald, M.C.2    Murphy, R.M.3
  • 13
    • 0028980362 scopus 로고
    • The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto C, Castano EM, Frangione B and Inestrosa NC (1995). The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270, 3063-3067
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 14
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E, Hölzemann G and Seelig J (1995). Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252, 633-642
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 15
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA and Teplow DB (1996). On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. 93, 1125-1129
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 17
    • 0028981219 scopus 로고
    • Structure-activity analysis of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG and Cotman CW (1995). Structure-activity analysis of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity. J. Neurochem. 64, 253-265
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 18
    • 0023473545 scopus 로고
    • Ten to fourteen residue peptides of Alzheimer's Disease protein are suffcient for amyloid fibril formation and its characteristic diffraction pattern
    • Gorévic PD, Castano EM, Sarma R and Frangione B (1987). Ten to fourteen residue peptides of Alzheimer's Disease protein are suffcient for amyloid fibril formation and its characteristic diffraction pattern. Biochem. Biophys. Res. Commun. 147, 854-862
    • (1987) Biochem. Biophys. Res. Commun. , vol.147 , pp. 854-862
    • Gorévic, P.D.1    Castano, E.M.2    Sarma, R.3    Frangione, B.4
  • 21
    • 0028181758 scopus 로고
    • Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35)
    • Terzi E, Hölzemann G and Seelig J (1994). Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35). Biochemistry 33, 1345-1350
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 22
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's Disease and scrapie?
    • Jarrett JT and Lansbury PT (1993). Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's Disease and scrapie? Cell 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 23
    • 0028096692 scopus 로고
    • Biochemical evidence for the long-tail form (Aβ1-43/43) of amyloid β protein as a seed molecule in cerebral deposits of Alzheimer's Disease
    • Tamaoka A, Kondo T, Odaka A, Sahara N, Sawamura N, Ozawa K, Suzuki N, Shoji S and Mori H (1994). Biochemical evidence for the long-tail form (Aβ1-43/43) of amyloid β protein as a seed molecule in cerebral deposits of Alzheimer's Disease. Biochem. Biophys. Res. Commun. 205, 834-842
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 834-842
    • Tamaoka, A.1    Kondo, T.2    Odaka, A.3    Sahara, N.4    Sawamura, N.5    Ozawa, K.6    Suzuki, N.7    Shoji, S.8    Mori, H.9
  • 24
    • 0027332081 scopus 로고
    • β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer's Disease
    • Roher AE, Lowenson JD, Clarke S, Woods AS, Cotter RJ, Gowing E and Ball MJ (1993). β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer's Disease. Proc. Natl. Acad. Sci. USA 90, 10836-10840
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 25
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial β protein precursor (βAPP717) mutants
    • Suzuki N, Cheung TT, Cai X-D, Odaka A, Otvos L, Eckman C, Golde TE and Younkin SG (1994). An increased percentage of long amyloid β protein secreted by familial β protein precursor (βAPP717) mutants. Science 264, 1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.-D.3    Odaka, A.4    Otvos, L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 26
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that the 42-and 40-amino acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities
    • Citron M, Diehl TS, Gordon G, Biere AL, Seubert P and Selkoe DJ (1996). Evidence that the 42-and 40-amino acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities. Proc. Natl. Acad. Sci. 93, 13170-13175
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13170-13175
    • Citron, M.1    Diehl, T.S.2    Gordon, G.3    Biere, A.L.4    Seubert, P.5    Selkoe, D.J.6
  • 28
    • 0028971326 scopus 로고
    • Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure
    • Soto C, Castaño EM, Kumar RA, Beavis RC and Frangione B (1995). Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci. Lett. 200, 105-108
    • (1995) Neurosci. Lett. , vol.200 , pp. 105-108
    • Soto, C.1    Castaño, E.M.2    Kumar, R.A.3    Beavis, R.C.4    Frangione, B.5
  • 31
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's Disease. Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PTM and Zagorski MG (1992). Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's Disease. Analysis of circular dichroism spectra. J. Mol. Biol. 225, 1075-1093
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.G.4
  • 32
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of β-amyloid peptide
    • Shen C-L and Murphy RM (1995). Solvent effects on self-assembly of β-amyloid peptide. Biophys. J. 69, 640-651
    • (1995) Biophys. J. , vol.69 , pp. 640-651
    • Shen, C.-L.1    Murphy, R.M.2
  • 34
    • 0030983405 scopus 로고    scopus 로고
    • Mechanisms of neurotoxicity with amyloid β deposition and the role of free radicals in the pathogenesis of Alzheimer's Disease. A critical appraisal
    • Sayre LM, Zagorski MG, Surewicz WK, Krafft GA and Perry G (1997). Mechanisms of neurotoxicity with amyloid β deposition and the role of free radicals in the pathogenesis of Alzheimer's Disease. A critical appraisal. Chem. Res. Toxicol. 10, 518-526
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 518-526
    • Sayre, L.M.1    Zagorski, M.G.2    Surewicz, W.K.3    Krafft, G.A.4    Perry, G.5
  • 35
    • 0026631361 scopus 로고
    • NMR Studies of Amyloid β-Peptides: Proton assignments, secondary structure, and mechanism of an α-helix⇒β-sheet conversion for a homologus, 28-residue, N-terminal fragment
    • Zagorski MG and Barrow CJ (1992). NMR Studies of Amyloid β-Peptides: Proton assignments, secondary structure, and mechanism of an α-helix⇒β-sheet conversion for a homologus, 28-residue, N-terminal fragment. Biochemistry 31, 5621-5631
    • (1992) Biochemistry , vol.31 , pp. 5621-5631
    • Zagorski, M.G.1    Barrow, C.J.2
  • 37
    • 0030457933 scopus 로고    scopus 로고
    • Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment
    • Kohno T, Kobayashi K, Maeda T, Saot K and Takashima A (1996). Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment. Biochemistry 35, 16094-16104
    • (1996) Biochemistry , vol.35 , pp. 16094-16104
    • Kohno, T.1    Kobayashi, K.2    Maeda, T.3    Saot, K.4    Takashima, A.5
  • 38
    • 0030983767 scopus 로고    scopus 로고
    • The interaction of β-amyloid protein fragment (12-28) with lipid environments
    • Fletcher TG and Keire DA (1997). The interaction of β-amyloid protein fragment (12-28) with lipid environments. Protein Science 6, 666-675
    • (1997) Protein Science , vol.6 , pp. 666-675
    • Fletcher, T.G.1    Keire, D.A.2
  • 39
    • 0005995412 scopus 로고
    • Efficient high yield reversed-phase HPLC separations of amyloid precursor polypeptide C-terminal fragments
    • Columbus, OH
    • Boyes BE, Efficient high yield reversed-phase HPLC separations of amyloid precursor polypeptide C-terminal fragments, 14th American Peptide Symposium, Columbus, OH, 1995.
    • (1995) 14th American Peptide Symposium
    • Boyes, B.E.1
  • 44
    • 0026692124 scopus 로고
    • Mass spectrometry of peptides and proteins
    • Biemann K (1992). Mass spectrometry of peptides and proteins. Annu. Rev. Biochem. 61, 977-1010
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 977-1010
    • Biemann, K.1
  • 48
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by fourier transform infrared spectroscopy: A critical assessment
    • Surewicz WK, Mantsch HH and Chapman D (1993). Determination of protein secondary structure by fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32, 389-394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 52
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner B, Duffy L and Kirschner D (1990). Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250, 279-282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.1    Duffy, L.2    Kirschner, D.3
  • 53
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson MP, Tomaselli KJ and Rydel RE (1993). Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res. 621, 35-49
    • (1993) Brain Res. , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 56
    • 0025371975 scopus 로고
    • Alzheimer's β-amyloid protein is covalently modified when dissolved in formic acid
    • Klunk WE and Pettegrew JW (1990). Alzheimer's β-amyloid protein is covalently modified when dissolved in formic acid. Journal of Neurochemistry 54, 2050-2056
    • (1990) Journal of Neurochemistry , vol.54 , pp. 2050-2056
    • Klunk, W.E.1    Pettegrew, J.W.2
  • 58
    • 0026650413 scopus 로고
    • Covalent modification of Alzheimer's amyloid β-peptide in formic acid solutions
    • Orlando R, Kenny PTM and Zagorski MG (1992). Covalent modification of Alzheimer's amyloid β-peptide in formic acid solutions. Biochem. Biophys. Res. Commun. 184, 686-691
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 686-691
    • Orlando, R.1    Kenny, P.T.M.2    Zagorski, M.G.3
  • 59
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J, Lorenzo A and Yanker BA (1992). Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging 13, 609-612
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yanker, B.A.3
  • 60
    • 0026570528 scopus 로고
    • β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I and Rydel RE (1992). β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. Res. 12, 376-389
    • (1992) J. Neurosci. Res. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 62
    • 0031018193 scopus 로고    scopus 로고
    • Conformations of β-amyloid in solution
    • Kaneko I and Tutumi S (1997). Conformations of β-amyloid in solution. J. Neurochem. 68, 438-439
    • (1997) J. Neurochem. , vol.68 , pp. 438-439
    • Kaneko, I.1    Tutumi, S.2
  • 63
    • 0028178837 scopus 로고
    • β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's Disease
    • Butterfield DA, Hensley K, Harris M, Mattson M and Carney J (1994). β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's Disease. Biochem. Biophys. Res. Commun. 200, 710-715
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.