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Biophys J, December 2000, p. 3282-3293, Vol. 79, No. 6
*Oxford Centre for Molecular Sciences, New Chemistry Laboratory,
and Inorganic Chemistry Laboratory, University of Oxford,
Oxford OX1 3QT, United Kingdom
Atomic force microscopy has been employed to investigate
the structural organization of amyloid fibrils produced in vitro from
three very different polypeptide sequences. The systems investigated are a 10-residue peptide derived from the sequence of transthyretin, the 90-residue SH3 domain of bovine phosphatidylinositol-3'-kinase, and
human wild-type lysozyme, a 130-residue protein containing four
disulfide bridges. The results demonstrate distinct similarities between the structures formed by the different classes of fibrils despite the contrasting nature of the polypeptide species involved. SH3
and lysozyme fibrils consist typically of four protofilaments, exhibiting a left-handed twist along the fibril axis. The substructure of TTR10-19 fibrils is not resolved by atomic force
microscopy and their uniform appearance is suggestive of a regular
self-association of very thin filaments. We propose that the exact
number and orientation of protofilaments within amyloid fibrils is
dictated by packing of the regions of the polypeptide chains that are
not directly involved in formation of the cross-
core of the
fibrils. The results obtained for these proteins, none of which is
directly associated with any human disease, are closely similar to
those of disease-related amyloid fibrils, supporting the concept that amyloid is a generic structure of polypeptide chains. The detailed architecture of an individual fibril, however, depends on the manner in
which the protofilaments assemble into the fibrillar structure, which
in turn is dependent on the sequence of the polypeptide and the
conditions under which the fibril is formed.
Biophys J, December 2000, p. 3282-3293, Vol. 79, No. 6
© 2000 by the Biophysical Society 0006-3495/00/12/3282/12 $2.00
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