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

Authors: Victoria L. Sedman; Stephanie Allen; Weng C. Chan; Martyn C. Davies; Clive J. Roberts; Saul J.B. Tendler; Philip M. Williams

Source: Protein and Peptide Letters, Volume 12, Number 1, January 2005 , pp. 79-83(5)

Publisher: Bentham Science Publishers

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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

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866053406129

Affiliations: 1: Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham, NG7 2RD,. UK.

Publication date: 2005-01-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.