Atomic force microscopy study of human amylin (20-29) fibrils

Sedman, Victoria L.; Allen, Stephanie; Chan, Weng C.; Davies, Martyn C.; Roberts, Clive J.; Tendler, Saul J.B.; Williams, Philip M.

doi:10.2174/0929866053406129

All Outputs (1)

Atomic force microscopy study of human amylin (20-29) fibrils (2005)
Journal Article
Sedman, V. L., Allen, S., Chan, W. C., Davies, M. C., Roberts, C. J., Tendler, S. J., & Williams, P. M. (2005). Atomic force microscopy study of human amylin (20-29) fibrils. Protein and Peptide Letters, 12(1), 79-83. https://doi.org/10.2174/0929866053406129

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... Read More about Atomic force microscopy study of human amylin (20-29) fibrils.