34th Annual Student Research Conference
The Effect of Curcumin on the Fibril Formation of Amyloid-β Fragments 1-16, 1-28, and 1-40
Valerie S. Winkler
Dr. Brittany Hagenhoff , Faculty Mentor
Alzheimer's disease involves the formation of interneuronal plaques that are heavily composed of fibrils of the 39-43 residue protein, amyloid-β (Aβ). Therefore, potential therapeutic measures have focused on disruption of Aβ fibril aggregation, such as the use of the polyphenol curcumin. A fluorescence assay was utilized to determine the fibril formation over time of different Aβ fragments, particularly 1-16, 1-28, and 1-40, as well as probe the effects of curcumin. While curcumin did not significantly affect formation of the Aβ 1-16 fibrils, there was an observed effect by curcumin on fibril formation for Aβ 1-28 and Aβ 1-40, suggesting that curcumin may affect Aβ fibril formation within the peptide residue range of 17-40. However, the fluorescence of curcumin when bound to Aβ was found to impact the methodological viability of fibril quantification, which shall be further analyzed.
Keywords: Amyloid-β, Analytical, Chemistry, Biochemistry, Curcumin, Protein, Spectroscopy, Aβ
Topic(s):Chemistry
Biochemistry and Molecular Biology
Presentation Type: Face-to-Face Oral Presentation
Session: 401-4
Location: SUB GEO
Time: 4:15