COLL 50 |
| Jed P. Aucoin1, Marcus A. Etienne1, Robert P. Hammer1, Mark L. McLaughlin1, Paul S. Russo2, and Robin L. McCarley1. (1) Department of Chemistry, Louisiana State University, 232 Choppin Hall, Baton Rouge, LA 70803, (2) Department of Chemistry and Macromolecular Studies Group, Louisiana State University, Baton Rouge, LA 70803 |
| Observations of morphological changes in Amyloid aggregation in vitro in the presence of a peptide–based aggregation inhibitor developed and synthesized by us are reported. Beta-Amyloid fibrils are a major constituent of the senile plaques located in Alzheimer–diseased brain tissue. Interruption of Amyloid fibril growth and intercalation of Amyloid fibrils by our inhibitor have been observed with scanning force microscopy and transmission electron microscopy. These observations have lead to further study of the occurrence and pathway of the inhibitor/Amyloid aggregate species. The microscopy work is complemented with fluorescent thioflavin-T binding measurements to better determine the interplay between inhibitor and beta-Amyloid 1-40. |
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Nanoscale Imaging of Biological Systems
Division of Colloid and Surface Chemistry |