On the structural definition of amyloid fibrils and other polypeptide aggregates |
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Authors: | M Fändrich |
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Institution: | Leibniz-Institut für Altersforschung, Beutenbergstrasse 11, 07745, Jena, Germany. fandrich@fli-leibniz.de |
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Abstract: | Amyloid fibrils occur inside the human body, associated with ageing or a group of diseases that includes, amongst others,
Alzheimer’s disease, atherosclerosis and type II diabetes. Many natural polypeptide chains are able to form amyloid fibrils
in vivo or in vitro, and this ability has been suggested to represent an inherent consequence of the chemical structure of the polypeptide chain.
Recent literature has provided a wealth of information about the structure of aggregates, precipitates, amyloid fibrils and
other types of fibrillar polypeptide assemblies. However, the biophysical meaning associated with these terms can differ considerably
depending on the context of their usage. This overview presents a structural comparison of amyloid fibrils and other types
of polypeptide assemblies and defines amyloid fibrils, based on structural considerations, as fibrillar polypeptide aggregates
with a cross-β conformation.
Received 1 March 2007; received after revision 15 March 2007; accepted 25 April 2007 |
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Keywords: | Amyloid conformational disease misfolding prion protein folding |
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