Title: Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils
Volume: 12
Issue: 1
Author(s): Victoria L. Sedman, Stephanie Allen, Weng C. Chan, Martyn C. Davies, Clive J. Roberts, Saul J.B. Tendler and Philip M. Williams
Affiliation:
Keywords:
protein aggregation, designability, protein folding, protein design, amyloid
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.
