Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bouchard, M.
Right arrow Articles by Robinson, C. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bouchard, M.
Right arrow Articles by Robinson, C. V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 9, Issue 10 1960-1967, Copyright © 2000 by The Protein Society

Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy [In Process Citation]

M Bouchard, J Zurdo, EJ Nettleton, CM Dobson and CV Robinson
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, United Kingdom.

Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD), and electron microscopy (EM) have been used simultaneously to follow the temperature-induced formation of amyloid fibrils by bovine insulin at acidic pH. The FTIR and CD data confirm that, before heating, insulin molecules in solution at pH 2.3 have a predominantly native-like alpha-helical structure. On heating to 70 degrees C, partial unfolding occurs and results initially in aggregates that are shown by CD and FT-IR spectra to retain a predominantly helical structure. Following this step, changes in the CD and FTIR spectra occur that are indicative of the extensive conversion of the molecular conformation from alpha-helical to beta-sheet structure. At later stages, EM shows the development of fibrils with well-defined repetitive morphologies including structures with a periodic helical twist of approximately 450 A. The results indicate that formation of fibrils by insulin requires substantial unfolding of the native protein, and that the most highly ordered structures result from a slow evolution of the morphology of the initially formed fibrillar species.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
M. I. Smith, J. S. Sharp, and C. J. Roberts
Insulin Fibril Nucleation: The Role of Prefibrillar Aggregates
Biophys. J., October 1, 2008; 95(7): 3400 - 3406.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
Z. Guo and D. Eisenberg
The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold
Protein Sci., September 1, 2008; 17(9): 1617 - 1623.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. S. P. Svane, K. Jahn, T. Deva, A. Malmendal, D. E. Otzen, J. Dittmer, and N. Chr. Nielsen
Early Stages of Amyloid Fibril Formation Studied by Liquid-State NMR: The Peptide Hormone Glucagon
Biophys. J., July 1, 2008; 95(1): 366 - 377.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
R. Gerber, A. Tahiri-Alaoui, P.J. Hore, and W. James
Conformational pH dependence of intermediate states during oligomerization of the human prion protein
Protein Sci., March 1, 2008; 17(3): 537 - 544.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. I. Smith, J. S. Sharp, and C. J. Roberts
Nucleation and Growth of Insulin Fibrils in Bulk Solution and at Hydrophobic Polystyrene Surfaces
Biophys. J., September 15, 2007; 93(6): 2143 - 2151.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. P. J. Knowles, W. Shu, G. L. Devlin, S. Meehan, S. Auer, C. M. Dobson, and M. E. Welland
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass
PNAS, June 12, 2007; 104(24): 10016 - 10021.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
K. L. De Jong, B. Incledon, C. M. Yip, and M. R. DeFelippis
Amyloid Fibrils of Glucagon Characterized by High-Resolution Atomic Force Microscopy
Biophys. J., September 1, 2006; 91(5): 1905 - 1914.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
Y. Cordeiro, J. Kraineva, M. C. Suarez, A. G. Tempesta, J. W. Kelly, J. L. Silva, R. Winter, and D. Foguel
Fourier Transform Infrared Spectroscopy Provides a Fingerprint for the Tetramer and for the Aggregates of Transthyretin
Biophys. J., August 1, 2006; 91(3): 957 - 967.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Bader, M. A. Seeliger, S. E. Kelly, L. L. Ilag, F. Meersman, A. Limones, B. F. Luisi, C. M. Dobson, and L. S. Itzhaki
Folding and Fibril Formation of the Cell Cycle Protein Cks1
J. Biol. Chem., July 7, 2006; 281(27): 18816 - 18824.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Manno, E. F. Craparo, V. Martorana, D. Bulone, and P. L. San Biagio
Kinetics of Insulin Aggregation: Disentanglement of Amyloid Fibrillation from Large-Size Cluster Formation
Biophys. J., June 15, 2006; 90(12): 4585 - 4591.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. S. Rogers, M. R. H. Krebs, E. H. C. Bromley, E. van der Linden, and A. M. Donald
Optical Microscopy of Growing Insulin Amyloid Spherulites on Surfaces In Vitro
Biophys. J., February 1, 2006; 90(3): 1043 - 1054.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
R. F. Pasternack, E. J. Gibbs, S. Sibley, L. Woodard, P. Hutchinson, J. Genereux, and K. Kristian
Formation Kinetics of Insulin-Based Amyloid Gels and the Effect of Added Metalloporphyrins
Biophys. J., February 1, 2006; 90(3): 1033 - 1042.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. Podesta, G. Tiana, P. Milani, and M. Manno
Early Events in Insulin Fibrillization Studied by Time-Lapse Atomic Force Microscopy
Biophys. J., January 15, 2006; 90(2): 589 - 597.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Huang, J. Dong, N. B. Phillips, P. R. Carey, and M. A. Weiss
Proinsulin Is Refractory to Protein Fibrillation: TOPOLOGICAL PROTECTION OF A PRECURSOR PROTEIN FROM CROSS-{beta} ASSEMBLY
J. Biol. Chem., December 23, 2005; 280(51): 42345 - 42355.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
F. Librizzi and C. Rischel
The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
Protein Sci., December 1, 2005; 14(12): 3129 - 3134.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Calamai, F. Chiti, and C. M. Dobson
Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein
Biophys. J., December 1, 2005; 89(6): 4201 - 4210.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
V. A. Goncharov
Mass Spectroscopic Analysis of Sup35NM Prion Polymerization
Biophys. J., December 1, 2005; 89(6): 4139 - 4148.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. R. H. Krebs, E. H. C. Bromley, S. S. Rogers, and A. M. Donald
The Mechanism of Amyloid Spherulite Formation by Bovine Insulin
Biophys. J., March 1, 2005; 88(3): 2013 - 2021.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
R. Jansen, W. Dzwolak, and R. Winter
Amyloidogenic Self-Assembly of Insulin Aggregates Probed by High Resolution Atomic Force Microscopy
Biophys. J., February 1, 2005; 88(2): 1344 - 1353.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
G. Zandomeneghi, M. R.H. Krebs, M. G. McCammon, and M. Fandrich
FTIR reveals structural differences between native {beta}-sheet proteins and amyloid fibrils
Protein Sci., December 1, 2004; 13(12): 3314 - 3321.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. R. H. Krebs, C. E. MacPhee, A. F. Miller, I. E. Dunlop, C. M. Dobson, and A. M. Donald
The formation of spherulites by amyloid fibrils of bovine insulin
PNAS, October 5, 2004; 101(40): 14420 - 14424.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
A. Arora, C. Ha, and C. B. Park
Insulin amyloid fibrillation at above 100{degrees}C: New insights into protein folding under extreme temperatures
Protein Sci., September 1, 2004; 13(9): 2429 - 2436.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
H.-H. Tsai, D. Zanuy, N. Haspel, K. Gunasekaran, B. Ma, C.-J. Tsai, and R. Nussinov
The Stability and Dynamics of the Human Calcitonin Amyloid Peptide DFNKF
Biophys. J., July 1, 2004; 87(1): 146 - 158.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. R.H. Krebs, L. A. Morozova-Roche, K. Daniel, C. V. Robinson, and C. M. Dobson
Observation of sequence specificity in the seeding of protein amyloid fibrils
Protein Sci., July 1, 2004; 13(7): 1933 - 1938.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
W. Dzwolak, V. Smirnovas, R. Jansen, and R. Winter
Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study
Protein Sci., July 1, 2004; 13(7): 1927 - 1932.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Q.-x. Hua and M. A. Weiss
Mechanism of Insulin Fibrillation: THE STRUCTURE OF INSULIN UNDER AMYLOIDOGENIC CONDITIONS RESEMBLES A PROTEIN-FOLDING INTERMEDIATE
J. Biol. Chem., May 14, 2004; 279(20): 21449 - 21460.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Necula, C. N. Chirita, and J. Kuret
Rapid Anionic Micelle-mediated {alpha}-Synuclein Fibrillization in Vitro
J. Biol. Chem., November 21, 2003; 278(47): 46674 - 46680.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. R. Nilsson and C. M. Dobson
Chemical modification of insulin in amyloid fibrils
Protein Sci., November 1, 2003; 12(11): 2637 - 2641.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Srisailam, T. K. S. Kumar, D. Rajalingam, K. M. Kathir, H.-S. Sheu, F.-J. Jan, P.-C. Chao, and C. Yu
Amyloid-like Fibril Formation in an All beta -Barrel Protein. PARTIALLY STRUCTURED INTERMEDIATE STATE(S) IS A PRECURSOR FOR FIBRIL FORMATION
J. Biol. Chem., May 9, 2003; 278(20): 17701 - 17709.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
B. Xu, Q.-X. Hua, S. H. Nakagawa, W. Jia, Y.-C. Chu, P. G. Katsoyannis, and M. A. Weiss
A cavity-forming mutation in insulin induces segmental unfolding of a surrounding {alpha}-helix
Protein Sci., January 1, 2002; 11(1): 104 - 116.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. E. Bevivino and P. J. Loll
An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils
PNAS, September 19, 2001; (2001) 211305198.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
D. P. Smith and S. E. Radford
Role of the single disulphide bond of {beta}2-microglobulin in amyloidosis in vitro
Protein Sci., September 1, 2001; 10(9): 1775 - 1784.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. E. Bevivino and P. J. Loll
An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils
PNAS, October 9, 2001; 98(21): 11955 - 11960.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.