TITLE

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

AUTHOR(S)
Sedman, Victoria L.; Allen, Stephanie; Chan, Weng C.; Davies, Martyn C.; Roberts, Clive J.; Tendler, Saul J. B.; Williams, Philip M.
PUB. DATE
January 2005
SOURCE
Protein & Peptide Letters;Jan2005, Vol. 12 Issue 1, p79
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
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.
ACCESSION #
15594373

 

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