X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin

Jarvis, J. A., Craik, D. J. and Wilce, M. C. J. (1993) X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin. Biochemical and Biophysical Research Communications, 192 3: 991-998. doi:10.1006/bbrc.1993.1514


Author Jarvis, J. A.
Craik, D. J.
Wilce, M. C. J.
Title X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 0006-291X
Publication date 1993-05
Sub-type Article (original research)
DOI 10.1006/bbrc.1993.1514
Volume 192
Issue 3
Start page 991
End page 998
Total pages 8
Place of publication Philadelphia, PA, United States
Publisher Elsevier
Language eng
Formatted abstract
Two synthetic peptide fragments of the plasma protein transthyretin (TTR), previously shown to form fibrillar structures in vitro, have been examined using electron microscopy and X-ray diffraction. The fibrils displayed all characteristics of cross β-sheet conformation with antiparallel strand spacing of 4.7 Å and intersheet spacings of 8 - 10 Å as well as reflections indicating further lateral repeating units. A third peptide containing a substitution equivalent to a mutation in TTR known to increase the propensity of TTR to form amyloid was also examined. It also formed fibrils and showed similar cross β-sheet structure, but with closer intersheet packing than its native equivalent.
Keyword Alzheimers-Disease
Beta-Protein
Amyloidosis
Invitro
Conformation
Secondary
Variant
Origin
Sheets
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
 
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