Atomic force microscopy study of human amylin (20-29) fibrils |
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| Authors: | Sedman Victoria L Allen Stephanie Chan Weng C Davies Martyn C Roberts Clive J Tendler Saul J B Williams Philip M |
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| Institution: | Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham. NG7 2RD UK. |
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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. |
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