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Volumn 404, Issue 2, 2010, Pages 337-352

The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils

Author keywords

Amyloid formation; Islet amyloid polypeptide; Protein aggregation; Protein sequence; Retro proteins

Indexed keywords

AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; PROTEINASE K;

EID: 78349308081     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.052     Document Type: Article
Times cited : (40)

References (61)
  • 2
    • 0029987096 scopus 로고    scopus 로고
    • Does a backwardly read protein sequence have a unique native state?
    • Olszewski K.A., Kolinski A., Skolnick J. Does a backwardly read protein sequence have a unique native state?. Protein Eng. 1996, 9:5-14.
    • (1996) Protein Eng. , vol.9 , pp. 5-14
    • Olszewski, K.A.1    Kolinski, A.2    Skolnick, J.3
  • 3
    • 0026779653 scopus 로고
    • Reversal of peptide backbone direction may result in the mirroring of protein structure
    • Guptasarma P. Reversal of peptide backbone direction may result in the mirroring of protein structure. FEBS Lett. 1992, 310:205-210.
    • (1992) FEBS Lett. , vol.310 , pp. 205-210
    • Guptasarma, P.1
  • 6
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 8
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L., Teng P.K., Riek R., Eisenberg D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl Acad. Sci. USA 2010, 107:3487-3492.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 9
    • 0037059069 scopus 로고    scopus 로고
    • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    • Chiti F., Calamai M., Taddei N., Stefani M., Ramponi G., Dobson C.M. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl Acad. Sci. USA 2002, 99:16419-16426.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5    Dobson, C.M.6
  • 10
    • 2442553006 scopus 로고    scopus 로고
    • Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
    • Ventura S., Zurdo J., Narayanan S., Parreno M., Mangues R., Reif B., et al. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc. Natl Acad. Sci. USA 2004, 101:7258-7263.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7258-7263
    • Ventura, S.1    Zurdo, J.2    Narayanan, S.3    Parreno, M.4    Mangues, R.5    Reif, B.6
  • 11
    • 0030779130 scopus 로고    scopus 로고
    • Amidation of beta-amyloid peptide strongly reduced the amyloidogenic activity without alteration of the neurotoxicity
    • Forloni G., Lucca E., Angeretti N., Della Torre P., Salmona M. Amidation of beta-amyloid peptide strongly reduced the amyloidogenic activity without alteration of the neurotoxicity. J. Neurochem. 1997, 69:2048-2054.
    • (1997) J. Neurochem. , vol.69 , pp. 2048-2054
    • Forloni, G.1    Lucca, E.2    Angeretti, N.3    Della Torre, P.4    Salmona, M.5
  • 12
    • 0027259274 scopus 로고
    • Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • Selvaggini C., De Gioia L., Cantu L., Ghibaudi E., Diomede L., Passerini F., et al. Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Biophys. Res. Commun. 1993, 194:1380-1386.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1380-1386
    • Selvaggini, C.1    De Gioia, L.2    Cantu, L.3    Ghibaudi, E.4    Diomede, L.5    Passerini, F.6
  • 13
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • Ross E.D., Baxa U., Wickner R.B. Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 2004, 24:7206-7213.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 15
  • 16
    • 34547646436 scopus 로고    scopus 로고
    • The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution
    • Monsellier E., Ramazzotti M., de Laureto P.P., Tartaglia G.G., Taddei N., Fontana A., et al. The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. Biophys. J. 2007, 93:4382-4391.
    • (2007) Biophys. J. , vol.93 , pp. 4382-4391
    • Monsellier, E.1    Ramazzotti, M.2    de Laureto, P.P.3    Tartaglia, G.G.4    Taddei, N.5    Fontana, A.6
  • 17
    • 33845624669 scopus 로고    scopus 로고
    • Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro
    • Liu Y., Wei H., Wang J., Qu J., Zhao W., Tao H. Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro. Biochem. Biophys. Res. Commun. 2007, 353:139-146.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 139-146
    • Liu, Y.1    Wei, H.2    Wang, J.3    Qu, J.4    Zhao, W.5    Tao, H.6
  • 18
    • 0034126660 scopus 로고    scopus 로고
    • Islet amyloid polypeptide in the islets of Langerhans: friend or foe?
    • Gebre-Medhin S., Olofsson C., Mulder H. Islet amyloid polypeptide in the islets of Langerhans: friend or foe?. Diabetologia 2000, 43:687-695.
    • (2000) Diabetologia , vol.43 , pp. 687-695
    • Gebre-Medhin, S.1    Olofsson, C.2    Mulder, H.3
  • 19
    • 0023189095 scopus 로고
    • Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes
    • Clark A., Cooper G.J., Lewis C.E., Morris J.F., Willis A.C., Reid K.B., Turner R.C. Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes. Lancet 1987, 2:231-234.
    • (1987) Lancet , vol.2 , pp. 231-234
    • Clark, A.1    Cooper, G.J.2    Lewis, C.E.3    Morris, J.F.4    Willis, A.C.5    Reid, K.B.6    Turner, R.C.7
  • 20
    • 35148821507 scopus 로고    scopus 로고
    • CSSP2: an improved method for predicting contact-dependent secondary structure propensity
    • Yoon S., Welsh W.J., Jung H., Yoo Y.D. CSSP2: an improved method for predicting contact-dependent secondary structure propensity. Comput. Biol. Chem. 2007, 31:373-377.
    • (2007) Comput. Biol. Chem. , vol.31 , pp. 373-377
    • Yoon, S.1    Welsh, W.J.2    Jung, H.3    Yoo, Y.D.4
  • 21
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin 20-29
    • Moriarty D.F., Raleigh D.P. Effects of sequential proline substitutions on amyloid formation by human amylin 20-29. Biochemistry 1999, 38:1811-1818.
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 22
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human amylin
    • Tracz S.M., Abedini A., Driscoll M., Raleigh D.P. Role of aromatic interactions in amyloid formation by peptides derived from human amylin. Biochemistry 2004, 43:15901-15908.
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 23
    • 0037341842 scopus 로고    scopus 로고
    • Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis
    • Scrocchi L.A., Ha K., Chen Y., Wu L., Wang F., Fraser P.E. Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis. J. Struct. Biol. 2003, 141:218-227.
    • (2003) J. Struct. Biol. , vol.141 , pp. 218-227
    • Scrocchi, L.A.1    Ha, K.2    Chen, Y.3    Wu, L.4    Wang, F.5    Fraser, P.E.6
  • 24
    • 48049085902 scopus 로고    scopus 로고
    • The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation
    • Gilead S., Gazit E. The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation. Exp. Diabetes Res. 2008, 2008:256954.
    • (2008) Exp. Diabetes Res. , vol.2008 , pp. 256954
    • Gilead, S.1    Gazit, E.2
  • 25
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin
    • Kajava A.V., Aebi U., Steven A.C. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 2005, 348:247-252.
    • (2005) J. Mol. Biol. , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 26
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR
    • Luca S., Yau W.M., Leapman R., Tycko R. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 2007, 46:13505-13522.
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 28
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 29
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia G.G., Cavalli A., Pellarin R., Caflisch A. Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci. 2005, 14:2723-2734.
    • (2005) Protein Sci. , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 30
  • 33
    • 34548756136 scopus 로고    scopus 로고
    • Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential
    • Zhang Z., Chen H., Lai L. Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential. Bioinformatics 2007, 23:2218-2225.
    • (2007) Bioinformatics , vol.23 , pp. 2218-2225
    • Zhang, Z.1    Chen, H.2    Lai, L.3
  • 34
    • 36248964819 scopus 로고    scopus 로고
    • The PASTA server for protein aggregation prediction
    • Trovato A., Seno F., Tosatto S.C. The PASTA server for protein aggregation prediction. Protein Eng. Des. Sel. 2007, 20:521-523.
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 521-523
    • Trovato, A.1    Seno, F.2    Tosatto, S.C.3
  • 35
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • Jaikaran E.T., Higham C.E., Serpell L.C., Zurdo J., Gross M., Clark A., Fraser P.E. Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 2001, 308:515-525.
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 38
    • 33749836310 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth, propagation, and adaptation
    • Ban T., Yamaguchi K., Goto Y. Direct observation of amyloid fibril growth, propagation, and adaptation. Acc. Chem. Res. 2006, 39:663-670.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 663-670
    • Ban, T.1    Yamaguchi, K.2    Goto, Y.3
  • 39
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 1993, 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 40
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation
    • Munishkina L.A., Henriques J., Uversky V.N., Fink A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 2004, 43:3289-3300.
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Uversky, V.N.3    Fink, A.L.4
  • 41
    • 0034284479 scopus 로고    scopus 로고
    • Kinetics of the formation and dissolution of Ni precipitates in a gibbsite/amorphous silica mixture
    • Scheckel K.G., Sparks D.L. Kinetics of the formation and dissolution of Ni precipitates in a gibbsite/amorphous silica mixture. J. Colloid Interface Sci. 2000, 229:222-229.
    • (2000) J. Colloid Interface Sci. , vol.229 , pp. 222-229
    • Scheckel, K.G.1    Sparks, D.L.2
  • 43
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo A., Razzaboni B., Weir G.C., Yankner B.A. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 1994, 368:756-760.
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3    Yankner, B.A.4
  • 44
    • 66849106554 scopus 로고    scopus 로고
    • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
    • Bartlett A.I., Radford S.E. An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms. Nat. Struct. Mol. Biol. 2009, 16:582-588.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 582-588
    • Bartlett, A.I.1    Radford, S.E.2
  • 45
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill K.A. Theory for the folding and stability of globular proteins. Biochemistry 1985, 24:1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 46
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications
    • Fersht A.R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA 1995, 92:10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 47
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson H.J., Wright P.E., Scheraga H.A. The role of hydrophobic interactions in initiation and propagation of protein folding. Proc. Natl Acad. Sci. USA 2006, 103:13057-13061.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3
  • 48
    • 33750962168 scopus 로고    scopus 로고
    • Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding
    • Le Duff C.S., Whittaker S.B., Radford S.E., Moore G.R. Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding. J. Mol. Biol. 2006, 364:824-835.
    • (2006) J. Mol. Biol. , vol.364 , pp. 824-835
    • Le Duff, C.S.1    Whittaker, S.B.2    Radford, S.E.3    Moore, G.R.4
  • 49
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000, 289:1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 50
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon M., Chang I., Mohanty S., Luheshi L.M., Dobson C.M., Vendruscolo M., Favrin G. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput. Biol. 2007, 3:1727-1738.
    • (2007) PLoS Comput. Biol. , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 52
    • 29344454454 scopus 로고    scopus 로고
    • Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure
    • Schwartz R., King J. Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure. Protein Sci. 2006, 15:102-112.
    • (2006) Protein Sci. , vol.15 , pp. 102-112
    • Schwartz, R.1    King, J.2
  • 53
    • 0345827608 scopus 로고    scopus 로고
    • Sequence determinants of amyloid fibril formation
    • de la Paz M.L., Serrano L. Sequence determinants of amyloid fibril formation. Proc. Natl Acad. Sci. USA 2004, 101:87-92.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 87-92
    • de la Paz, M.L.1    Serrano, L.2
  • 55
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of beta-turn in proteins
    • Wilmot C.M., Thornton J.M. Analysis and prediction of the different types of beta-turn in proteins. J. Mol. Biol. 1988, 203:221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 56
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier E., Chiti F. Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep. 2007, 8:737-742.
    • (2007) EMBO Rep. , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 59
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method: 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method: 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 1988, 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 60
    • 0038795608 scopus 로고    scopus 로고
    • An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
    • Sabate R., Gallardo M., Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 2003, 71:190-195.
    • (2003) Biopolymers , vol.71 , pp. 190-195
    • Sabate, R.1    Gallardo, M.2    Estelrich, J.3


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