1H NMR analysis of fibril-forming peptide fragments of transthyretin

Jarvis, J. A., Kirkpatrick, A. and Craik, D. J. (1994) 1H NMR analysis of fibril-forming peptide fragments of transthyretin. International Journal of Peptide and Protein Research, 44 4: 388-398.

Author Jarvis, J. A.
Kirkpatrick, A.
Craik, D. J.
Title 1H NMR analysis of fibril-forming peptide fragments of transthyretin
Formatted title
1H NMR analysis of fibril-forming peptide fragments of transthyretin
Journal name International Journal of Peptide and Protein Research   Check publisher's open access policy
ISSN 0367-8377
Publication date 1994-10
Sub-type Article (original research)
Volume 44
Issue 4
Start page 388
End page 398
Total pages 11
Publisher Wiley-Blackwell
Language eng
Formatted abstract
Peptide fragments of the protein transthyretin, previously shown to form cross,B-sheet amyloid-like fibrils in vino, were investigated using 1H 1D and 2D NMR techniques. TTR 10-20, TTR 105-115 as well as a substituted analogue, (TTR 105-115(Met111) all formed amyloid-like fibrils readily in 20-30% acetonitrile/water at room temperature. It was found that the presence of fibrils in the peptide solutions did not affect the observable NMR spectra, which may have been due to the line-broadening that would be associated with these macromolecular species. 1H NMR spectra were thus representative of the monomeric form of the peptide in solution. Information from D2O exchange, 3J(NH-αH) coupling measurements, temperature coefficients and NOESY experiments suggested that these peptides have some propensity for turn or helix but were predominantly unstructured. There was no indication of the monomeric species existing predominantly in an extended form, suggesting that the formation of β-sheet based fibrils does not require preformed extended structures. TTR 105-115(Met111) displayed slight structural differences from TTR 105-115 which may be related to the fibril-forming propensity of the corresponding mutant TTR.
Keyword Amyloid Fibril
Nuclear Magnetic Resonance
Protein Secondary Structure
Amyloid Beta-Peptides
Solution Conformations
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 25 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Fri, 09 Sep 2011, 19:00:31 EST by System User on behalf of Institute for Molecular Bioscience