This Article Full Text Full Text (PDF) Supplement All Versions of this Article: biophysj.107.125146v1 94/7/L45    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Vaiana, S. M. Articles by Hofrichter, J. PubMed PubMed Citation Articles by Vaiana, S. M. Articles by Hofrichter, J.

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).