Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils
Victoria L. Sedman,
Weng C. Chan,
Martyn C. Davies,
Clive J. Roberts,
Saul J.B. Tendler,
Philip M. Williams.
Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our results demonstrate that the amylin(20-29) peptide fragment forms amyloid-like fibrils that display polymorphic structures. Twisting along the axis of fibrils was often observed in fibrils aged for 6 hours but disappeared in mature fibrils aged for longer time periods.
Keywords: protein aggregation, designability, protein folding, protein design, amyloid
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