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2000
Volume 12, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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.

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/content/journals/ppl/10.2174/0929866053406129
2005-01-01
2025-05-24
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  • Article Type:
    Review Article
Keyword(s): amyloid; designability; protein aggregation; protein design; protein folding
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