Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers |
| |
| Authors: | Vaiana Sara M Ghirlando Rodolfo Yau Wai-Ming Eaton William A Hofrichter James |
| |
| Affiliation: | * Laboratory of Chemical Physics, National Institute of Digestive and Diabetes and Kidney Diseases, National Institutes of Health, Bethesda, Maryland
† Laboratory of Molecular Biology, National Institute of Digestive and Diabetes and Kidney Diseases, National Institutes of Health, Bethesda, Maryland |
| |
| Abstract: | 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). |
| |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
|
