Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils

Author(s): Victoria L. Sedman, Stephanie Allen, Weng C. Chan, Martyn C. Davies, Clive J. Roberts, Saul J.B. Tendler, Philip M. Williams.

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 1 , 2005

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Abstract:

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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Article Details

VOLUME: 12
ISSUE: 1
Year: 2005
Page: [79 - 83]
Pages: 5
DOI: 10.2174/0929866053406129

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