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Sedimentation Studies on Human Amylin Fail to Detect Low-Molecular-Weight Oligomers

Sara M. Vaiana ^*, Rodolfo Ghirlando , Wai-Ming Yau ^*, William A. Eaton ^* and James Hofrichter ^*

^* Laboratory of Chemical Physics and Laboratory of Molecular Biology, National Institute of Digestive and Diabetes and Kidney Diseases, National Institutes of Health, Bethesda, Maryland

Correspondence: Address reprint requests and inquiries to James Hofrichter, Tel.: 301-496-6033; E-mail: jameshof{at}niddk.nih.gov.

Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloid-polypeptide. No oligomers containing <100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Aβ(1-42).