메뉴 건너뛰기




Volumn 45, Issue 26, 2006, Pages 8143-8151

New insights into the self-assembly of insulin amyloid fibrils: An H-D exchange FT-IR study

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; INSULIN; NANOTUBES; PROTONS;

EID: 33745610089     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060341a     Document Type: Article
Times cited : (61)

References (45)
  • 1
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N., and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: The importance of being unfolded, Biochim. Biophys. Acta 1698, 131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 3
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin: Even an ordinary globular protein can assume a rogue guise if conditions are right
    • Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin: Even an ordinary globular protein can assume a rogue guise if conditions are right, Nature 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 4
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M., and Dobson, C. M. (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation, EMBO J. 21, 5682-5690.
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 6
    • 17144398382 scopus 로고    scopus 로고
    • Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high-resolution hydrogen/deuterium exchange monitored by mass spectrometry
    • Nazabal, A., Maddelein, M. L., Bonneu, M., Saupe, S. J., and Schmitter, J. M. (2005) Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high-resolution hydrogen/deuterium exchange monitored by mass spectrometry, J. Biol. Chem. 280, 13220-13228.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13220-13228
    • Nazabal, A.1    Maddelein, M.L.2    Bonneu, M.3    Saupe, S.J.4    Schmitter, J.M.5
  • 8
    • 0344603844 scopus 로고    scopus 로고
    • The hydrogen exchange core and protein folding
    • Li, R. H., and Woodward, C. (1999) The hydrogen exchange core and protein folding, Protein Sci. 8, 1571-1590.
    • (1999) Protein Sci. , vol.8 , pp. 1571-1590
    • Li, R.H.1    Woodward, C.2
  • 9
    • 0033986637 scopus 로고    scopus 로고
    • D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding
    • Krantz, B. A., Moran, L. B., Kentsis, A., and Sosnick, T. R. (2000) D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding, Nat. Struct. Biol. 7, 62-71.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 62-71
    • Krantz, B.A.1    Moran, L.B.2    Kentsis, A.3    Sosnick, T.R.4
  • 12
    • 15544388942 scopus 로고    scopus 로고
    • Hydrogen-deuterium (H/D) exchange mapping of A-β(1-40) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
    • Wnittemore, N. A., Mishra, R., Kheterpal, I., Williams, A. D., Wetzel, R., and Serpersu, E. H. (2005) Hydrogen-deuterium (H/D) exchange mapping of A-β(1-40) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy, Biochemistry 44, 4434-4441.
    • (2005) Biochemistry , vol.44 , pp. 4434-4441
    • Wnittemore, N.A.1    Mishra, R.2    Kheterpal, I.3    Williams, A.D.4    Wetzel, R.5    Serpersu, E.H.6
  • 13
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of α-synuclein and other amyloids determined at the amino acid level
    • Del Mar, C., Greenbaum, E. A., Mayne, L., Englander, S. W., and Woods, V. L. (2005) Structure and properties of α-synuclein and other amyloids determined at the amino acid level, Proc. Natl. Acad. Sci. U.S.A. 102, 15477-15482.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 14
    • 0345060507 scopus 로고    scopus 로고
    • Aβ protofibrils possess a stable core structure resistant to hydrogen exchange
    • Kheterpal, I., Lashuel, H. A., Hartley, D. M., Wlaz, T., Lansbury, P. T., and Wetzel, R. (2003) Aβ protofibrils possess a stable core structure resistant to hydrogen exchange, Biochemistry 42, 14092-14098.
    • (2003) Biochemistry , vol.42 , pp. 14092-14098
    • Kheterpal, I.1    Lashuel, H.A.2    Hartley, D.M.3    Wlaz, T.4    Lansbury, P.T.5    Wetzel, R.6
  • 15
    • 0034692877 scopus 로고    scopus 로고
    • Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: A site-specific investigation by mass spectrometry
    • Tito, P., Nettleton, E. J., and Robinson, C. V. (2000) Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: A site-specific investigation by mass spectrometry, J. Mol. Biol. 303, 267-278.
    • (2000) J. Mol. Biol. , vol.303 , pp. 267-278
    • Tito, P.1    Nettleton, E.J.2    Robinson, C.V.3
  • 16
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandpmeneghi, G., Krebs, M. R. H., Mccammon, M. G., and Fahdrich, M. (2004) FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils, Protein Sci. 13, 3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandpmeneghi, G.1    Krebs, M.R.H.2    Mccammon, M.G.3    Fahdrich, M.4
  • 17
    • 3042665537 scopus 로고    scopus 로고
    • Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study
    • Dzwolak, W., Smirnovas, V., Jansen, R., and Winter, R. (2004) Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study, Protein Sci. 13, 1927-1932.
    • (2004) Protein Sci. , vol.13 , pp. 1927-1932
    • Dzwolak, W.1    Smirnovas, V.2    Jansen, R.3    Winter, R.4
  • 18
    • 0141567910 scopus 로고    scopus 로고
    • Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy
    • Dzwolak, W., Ravindra, R., Lendermann, J., and Winter, R. (2003) Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy, Biochemistry 42, 11347-11355.
    • (2003) Biochemistry , vol.42 , pp. 11347-11355
    • Dzwolak, W.1    Ravindra, R.2    Lendermann, J.3    Winter, R.4
  • 21
  • 23
    • 0028344969 scopus 로고
    • Equilibrium intermediates in the denaturation of human insulin and two monomeric insulin analogs
    • Millican, R. L., and Brems, D. N. (1994) Equilibrium intermediates in the denaturation of human insulin and two monomeric insulin analogs, Biochemistry 33, 1116-1124.
    • (1994) Biochemistry , vol.33 , pp. 1116-1124
    • Millican, R.L.1    Brems, D.N.2
  • 24
    • 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., Uversky, V. N., and Fink, A. L. (2001) Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism, Biochemistry 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    Uversky, V.N.7    Fink, A.L.8
  • 26
    • 2442468092 scopus 로고    scopus 로고
    • Stimulation of insulin fibrillation by urea-induced intermediates
    • Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2004) Stimulation of insulin fibrillation by urea-induced intermediates, J. Biol. Chem. 279, 14999-15013.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14999-15013
    • Ahmad, A.1    Millett, I.S.2    Doniach, S.3    Uversky, V.N.4    Fink, A.L.5
  • 27
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • Sluzky, V., Tamada, J. A., Klibanov, A. M., and Langer, R. (1991) Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces, Proc. Natl. Acad. Sci. U.S.A. 88, 9377-9381.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 31
    • 4344648815 scopus 로고    scopus 로고
    • Insulin amyloid fibrillation at above 100 °C: New insights into protein folding under extreme temperatures
    • Arora, A., Ha, C., and Park, C. B. (2004) Insulin amyloid fibrillation at above 100 °C: New insights into protein folding under extreme temperatures, Protein Sci. 13, 2429-2436.
    • (2004) Protein Sci. , vol.13 , pp. 2429-2436
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 34
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth, A. (2000) The infrared absorption of amino acid side chains, Prog. Biophys. Mol. Biol. 74, 141-173.
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 36
    • 0037085812 scopus 로고    scopus 로고
    • Isotope effects in liquid water by infrared spectroscopy
    • Max, J. J., and Chapados, C. (2002) Isotope effects in liquid water by infrared spectroscopy, J. Chem. Phys. 116, 4626-4642.
    • (2002) J. Chem. Phys. , vol.116 , pp. 4626-4642
    • Max, J.J.1    Chapados, C.2
  • 37
    • 0026469169 scopus 로고
    • Application of Fourier transform infrared spectroscopy to studies of aqueous protein solutions
    • Zuber, G., Prestrelski, S. J., and Benedek, K. (1992) Application of Fourier transform infrared spectroscopy to studies of aqueous protein solutions, Anal. Biochem. 207, 150-156.
    • (1992) Anal. Biochem. , vol.207 , pp. 150-156
    • Zuber, G.1    Prestrelski, S.J.2    Benedek, K.3
  • 38
    • 0024467352 scopus 로고
    • Conformational transitions in poly(L-lysine): Studies using Fourier transform infrared spectroscopy
    • Jackson, M., Haris, P. I., and Chapman, D. (1989) Conformational transitions in poly(L-lysine): Studies using Fourier transform infrared spectroscopy, Biochim. Biophys. Acta 998, 75-79.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 75-79
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 39
    • 0038461955 scopus 로고    scopus 로고
    • Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils
    • Dong, J., Wan, Z., Popov, M., Carey, P. R., and Weiss, M. A. (2003) Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils, J. Mol. Biol. 330, 431-442.
    • (2003) J. Mol. Biol. , vol.330 , pp. 431-442
    • Dong, J.1    Wan, Z.2    Popov, M.3    Carey, P.R.4    Weiss, M.A.5
  • 40
    • 0034646573 scopus 로고    scopus 로고
    • Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
    • MacPhee, C. E., and Dobson, C. M. (2000) Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin, J. Mol. Biol. 297, 1203-1215.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1203-1215
    • MacPhee, C.E.1    Dobson, C.M.2
  • 42
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J. L., Guijarro, J. L., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., and Saibil, H. R. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing, EMBO J. 18, 815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.L.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 44
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high-resolution atomic force microscopy
    • Jansen, R., Dzwolak, W., and Winter, R. (2005) Amyloidogenic self-assembly of insulin aggregates probed by high-resolution atomic force microscopy, Biophys. J. 88, 1344-1353.
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 45
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y., and Eisenberg, D. (2002) 3D domain swapping: As domains continue to swap, Protein Sci. 11, 1285-1299.
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.