The amyloid fibril field is briefly described, with some stress put on differences between various proteins and possible role for domain swapping. In the main body of the text, first, a short review is given of the folding properties of both human stefins, α/β-type globular proteins of 53% identity with a known three-dimensional fold. Second, in vitro study of amyloid fibril formation by human stefin B (type I cystatin) is described. Solvents of pH 4.8 and pH 3.3 with and without 2,2,2-trifluoroethanol (TFE) were probed, as it has been shown previously that stefin B forms acid intermediates, a native-like and molten globule intermediate, respectively. The kinetics of fibrillation were measured by thioflavin T fluorescence and CD. At pH 3.3, the protein is initially in the molten globule state. The fibrillation is faster than at pH 4.8; however, there is more aggregation observed. On adding TFE at each pH, the fibril formation is further accelerated.
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Conference Article|
August 01 2002
Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state
E. Žerovnik;
E. Žerovnik
1
*Department of Biochemistry and Molecular Biology, J. Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
1To whom correspondence should be addressed (e-mail eva.zerovnik@ijs.si)
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V. Turk;
V. Turk
*Department of Biochemistry and Molecular Biology, J. Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
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J. P. Waltho
J. P. Waltho
†Department of Molecular Biology and Biotechnology, Krebs Institute, Western Bank, University of Sheffield, Sheffield S10 2TN, U.K.
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Publisher: Portland Press Ltd
Received:
March 11 2002
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (4): 543–547.
Article history
Received:
March 11 2002
Citation
E. Žerovnik, V. Turk, J. P. Waltho; Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state. Biochem Soc Trans 1 August 2002; 30 (4): 543–547. doi: https://doi.org/10.1042/bst0300543
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