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Biophys. J. BioFAST: First Published January 25, 2008. doi:10.1529/biophysj.107.125146
© 2008 by the Biophysical Society.

A more recent version of this article appeared on April 1, 2008.
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BIOPHYSICAL LETTERS

Sedimentation studies on human amylin fail to detect low molecular weight oligomers

Sara M Vaiana 1, Rodolfo Ghirlando 2, Wai-Ming Yau 1, William A Eaton 1 and James Hofrichter 1*

1 Laboratory of Chemical Physics, National Institutes of Health
2 Laboratory of Molecular Biology, National Institutes of Health

* To whom correspondence should be addressed. E-mail: jameshof{at}niddk.nih.gov.

Submitted on November 2, 2007
Revised on November 30, 2007
Accepted on 13 December 2007


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

Key Words: amylin, amyloid, assembly, nucleation






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Copyright © 2008 by the Biophysical Society.