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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and Philip M. Williams

Volume 12, Issue 1, 2005

Page: [79 - 83] Pages: 5

DOI: 10.2174/0929866053406129

Price: $65

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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