Atomic force microscopy study of human amylin (20-29) fibrils

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

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.

Citation

Sedman, V. L., Allen, S., Chan, W. C., Davies, M. C., Roberts, C. J., Tendler, S. J., & Williams, P. M. (2005). Atomic force microscopy study of human amylin (20-29) fibrils. Protein and Peptide Letters, 12(1), 79-83. https://doi.org/10.2174/0929866053406129

• Journal Article Type: Article
• Publication Date: Jan 1, 2005
• Deposit Date: May 12, 2023
• Journal: Protein and Peptide Letters
• Print ISSN: 0929-8665
• Electronic ISSN: 1875-5305
• Publisher: Bentham Science Publishers
• Peer Reviewed: Peer Reviewed
• Volume: 12
• Issue: 1
• Pages: 79-83
• DOI: https://doi.org/10.2174/0929866053406129
• Public URL: https://nottingham-repository.worktribe.com/output/3137756
• Publisher URL: http://www.eurekaselect.com/article/24065